subject:(HEME HEMIN PROTOHEME BIOCHEMISTRY )

ETH Zürich

1. Schulz, Henk. A heme delivery pathway for cytochrome c maturation in Escherichia coli.

Degree: 2000, ETH Zürich

URL: http://hdl.handle.net/20.500.11850/144804

Subjects/Keywords: HÄM + HÄMIN + PROTOHÄM (BIOCHEMIE); CYTOCHROM-C (PROTEINE, PEPTIDE); ESCHERICHIA (MIKROBIOLOGIE); HEME + HEMIN + PROTOHEME (BIOCHEMISTRY); CYTOCHROME C (PROTEINS AND PEPTIDES); ESCHERICHIA (MICROBIOLOGY); info:eu-repo/classification/ddc/570; Life sciences

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Schulz, H. (2000). A heme delivery pathway for cytochrome c maturation in Escherichia coli. (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/144804

Chicago Manual of Style (16^th Edition):

Schulz, Henk. “A heme delivery pathway for cytochrome c maturation in Escherichia coli.” 2000. Doctoral Dissertation, ETH Zürich. Accessed March 05, 2021. http://hdl.handle.net/20.500.11850/144804.

MLA Handbook (7^th Edition):

Schulz, Henk. “A heme delivery pathway for cytochrome c maturation in Escherichia coli.” 2000. Web. 05 Mar 2021.

Vancouver:

Schulz H. A heme delivery pathway for cytochrome c maturation in Escherichia coli. [Internet] [Doctoral dissertation]. ETH Zürich; 2000. [cited 2021 Mar 05]. Available from: http://hdl.handle.net/20.500.11850/144804.

Council of Science Editors:

Schulz H. A heme delivery pathway for cytochrome c maturation in Escherichia coli. [Doctoral Dissertation]. ETH Zürich; 2000. Available from: http://hdl.handle.net/20.500.11850/144804

ETH Zürich

2. Christensen, Olaf. CcmA and CcmB, an ABC transporter involved in cytochrome c maturation.

Degree: 2005, ETH Zürich

URL: http://hdl.handle.net/20.500.11850/148784

Subjects/Keywords: CYTOCHROM-C (PROTEINE, PEPTIDE); ABC-TRANSPORTER (PROTEINE, PEPTIDE); HÄM + HÄMIN + PROTOHÄM (BIOCHEMIE); ESCHERICHIA (MIKROBIOLOGIE); CYTOCHROME C (PROTEINS AND PEPTIDES); ABC-TRANSPORTER (PROTEINS AND PEPTIDES); HEME + HEMIN + PROTOHEME (BIOCHEMISTRY); ESCHERICHIA (MICROBIOLOGY); info:eu-repo/classification/ddc/570; Life sciences

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Christensen, O. (2005). CcmA and CcmB, an ABC transporter involved in cytochrome c maturation. (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/148784

Chicago Manual of Style (16^th Edition):

Christensen, Olaf. “CcmA and CcmB, an ABC transporter involved in cytochrome c maturation.” 2005. Doctoral Dissertation, ETH Zürich. Accessed March 05, 2021. http://hdl.handle.net/20.500.11850/148784.

MLA Handbook (7^th Edition):

Christensen, Olaf. “CcmA and CcmB, an ABC transporter involved in cytochrome c maturation.” 2005. Web. 05 Mar 2021.

Vancouver:

Christensen O. CcmA and CcmB, an ABC transporter involved in cytochrome c maturation. [Internet] [Doctoral dissertation]. ETH Zürich; 2005. [cited 2021 Mar 05]. Available from: http://hdl.handle.net/20.500.11850/148784.

Council of Science Editors:

Christensen O. CcmA and CcmB, an ABC transporter involved in cytochrome c maturation. [Doctoral Dissertation]. ETH Zürich; 2005. Available from: http://hdl.handle.net/20.500.11850/148784

ETH Zürich

3. Ahuja, Umesh. Dynamics of heme delivery and protein-protein interactions during cytochrome c maturation.

Degree: 2005, ETH Zürich

URL: http://hdl.handle.net/20.500.11850/148799

Subjects/Keywords: CYTOCHROM-C (PROTEINE, PEPTIDE); HÄM + HÄMIN + PROTOHÄM (BIOCHEMIE); ESCHERICHIA (MIKROBIOLOGIE); PROTEIN-PROTEIN-WECHSELWIRKUNGEN; CYTOCHROME C (PROTEINS AND PEPTIDES); HEME + HEMIN + PROTOHEME (BIOCHEMISTRY); ESCHERICHIA (MICROBIOLOGY); PROTEIN-PROTEIN INTERACTIONS; info:eu-repo/classification/ddc/570; Life sciences

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Ahuja, U. (2005). Dynamics of heme delivery and protein-protein interactions during cytochrome c maturation. (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/148799

Chicago Manual of Style (16^th Edition):

Ahuja, Umesh. “Dynamics of heme delivery and protein-protein interactions during cytochrome c maturation.” 2005. Doctoral Dissertation, ETH Zürich. Accessed March 05, 2021. http://hdl.handle.net/20.500.11850/148799.

MLA Handbook (7^th Edition):

Ahuja, Umesh. “Dynamics of heme delivery and protein-protein interactions during cytochrome c maturation.” 2005. Web. 05 Mar 2021.

Vancouver:

Ahuja U. Dynamics of heme delivery and protein-protein interactions during cytochrome c maturation. [Internet] [Doctoral dissertation]. ETH Zürich; 2005. [cited 2021 Mar 05]. Available from: http://hdl.handle.net/20.500.11850/148799.

Council of Science Editors:

Ahuja U. Dynamics of heme delivery and protein-protein interactions during cytochrome c maturation. [Doctoral Dissertation]. ETH Zürich; 2005. Available from: http://hdl.handle.net/20.500.11850/148799

ETH Zürich

4. Alvino, Claudio. Sulla conversione della vitamina K-1 (fillochinone) negli embrioni di pollo e della vitamina K-3 (menadione) nel Lumbricus terrestris in vitamina K-2(20).

Degree: 1965, ETH Zürich

URL: http://hdl.handle.net/20.500.11850/133140

Subjects/Keywords: PHYLLOCHINONE, VITAMIN-K1 (BIOCHEMIE); PROVITAMIN-K, VITAMIN-K3, MENADION (BIOCHEMIE); VITAMINMETABOLISMUS (BIOCHEMIE); HÄM + HÄMIN + PROTOHÄM (BIOCHEMIE); PHYLLOQUINONES, VITAMIN K1 (BIOCHEMISTRY); PROVITAMIN K, VITAMIN K3, MENADIONE (BIOCHEMISTRY); VITAMIN METABOLISM (BIOCHEMISTRY); HEME + HEMIN + PROTOHEME (BIOCHEMISTRY); info:eu-repo/classification/ddc/570; info:eu-repo/classification/ddc/590; Life sciences; Zoological sciences

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Alvino, C. (1965). Sulla conversione della vitamina K-1 (fillochinone) negli embrioni di pollo e della vitamina K-3 (menadione) nel Lumbricus terrestris in vitamina K-2(20). (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/133140

Chicago Manual of Style (16^th Edition):

Alvino, Claudio. “Sulla conversione della vitamina K-1 (fillochinone) negli embrioni di pollo e della vitamina K-3 (menadione) nel Lumbricus terrestris in vitamina K-2(20).” 1965. Doctoral Dissertation, ETH Zürich. Accessed March 05, 2021. http://hdl.handle.net/20.500.11850/133140.

MLA Handbook (7^th Edition):

Alvino, Claudio. “Sulla conversione della vitamina K-1 (fillochinone) negli embrioni di pollo e della vitamina K-3 (menadione) nel Lumbricus terrestris in vitamina K-2(20).” 1965. Web. 05 Mar 2021.

Vancouver:

Alvino C. Sulla conversione della vitamina K-1 (fillochinone) negli embrioni di pollo e della vitamina K-3 (menadione) nel Lumbricus terrestris in vitamina K-2(20). [Internet] [Doctoral dissertation]. ETH Zürich; 1965. [cited 2021 Mar 05]. Available from: http://hdl.handle.net/20.500.11850/133140.

Council of Science Editors:

Alvino C. Sulla conversione della vitamina K-1 (fillochinone) negli embrioni di pollo e della vitamina K-3 (menadione) nel Lumbricus terrestris in vitamina K-2(20). [Doctoral Dissertation]. ETH Zürich; 1965. Available from: http://hdl.handle.net/20.500.11850/133140

ETH Zürich

5. Zeltina, Antra. Mechanistic studies of ABC transporter HmuUV-T facilitating heme uptake in Yersinia pestis.

Degree: 2013, ETH Zürich

URL: http://hdl.handle.net/20.500.11850/78373

Subjects/Keywords: IRON AND IRON CONTAINING COMPOUNDS (BIOCHEMISTRY); HEME + HEMIN + PROTOHEME (BIOCHEMISTRY); ABC-TRANSPORTER (PROTEINS AND PEPTIDES); HÄM + HÄMIN + PROTOHÄM (BIOCHEMIE); EISEN UND EISENHALTIGE SUBSTANZEN (BIOCHEMIE); YERSINIA (MIKROBIOLOGIE); YERSINIA (MICROBIOLOGY); ABC-TRANSPORTER (PROTEINE, PEPTIDE); info:eu-repo/classification/ddc/570; info:eu-repo/classification/ddc/570; Life sciences; Life sciences

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Zeltina, A. (2013). Mechanistic studies of ABC transporter HmuUV-T facilitating heme uptake in Yersinia pestis. (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/78373

Chicago Manual of Style (16^th Edition):

Zeltina, Antra. “Mechanistic studies of ABC transporter HmuUV-T facilitating heme uptake in Yersinia pestis.” 2013. Doctoral Dissertation, ETH Zürich. Accessed March 05, 2021. http://hdl.handle.net/20.500.11850/78373.

MLA Handbook (7^th Edition):

Zeltina, Antra. “Mechanistic studies of ABC transporter HmuUV-T facilitating heme uptake in Yersinia pestis.” 2013. Web. 05 Mar 2021.

Vancouver:

Zeltina A. Mechanistic studies of ABC transporter HmuUV-T facilitating heme uptake in Yersinia pestis. [Internet] [Doctoral dissertation]. ETH Zürich; 2013. [cited 2021 Mar 05]. Available from: http://hdl.handle.net/20.500.11850/78373.

Council of Science Editors:

Zeltina A. Mechanistic studies of ABC transporter HmuUV-T facilitating heme uptake in Yersinia pestis. [Doctoral Dissertation]. ETH Zürich; 2013. Available from: http://hdl.handle.net/20.500.11850/78373

ETH Zürich

6. Enggist, Elisabeth. The puzzle of cytochrome C biogenesis: structure and function of the heme chaperone CcmE.

Degree: 2003, ETH Zürich

URL: http://hdl.handle.net/20.500.11850/147390

Subjects/Keywords: HÄM + HÄMIN + PROTOHÄM (BIOCHEMIE); CYTOCHROM-C (PROTEINE, PEPTIDE); BIOGENESE, URSPRUNG DES LEBENS (PHYLOGENESE, BIOLOGIE); MOLEKULARE CHAPERONE (PROTEINE UND PEPTIDE); HEME + HEMIN + PROTOHEME (BIOCHEMISTRY); CYTOCHROME C (PROTEINS AND PEPTIDES); BIOGENESIS, ORIGIN OF LIFE (PHYLOGENESIS, BIOLOGY); MOLECULAR CHAPERONES (PROTEINS AND PEPTIDES); info:eu-repo/classification/ddc/570; Life sciences

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Enggist, E. (2003). The puzzle of cytochrome C biogenesis: structure and function of the heme chaperone CcmE. (Doctoral Dissertation). ETH Zürich. Retrieved from http://hdl.handle.net/20.500.11850/147390

Chicago Manual of Style (16^th Edition):

Enggist, Elisabeth. “The puzzle of cytochrome C biogenesis: structure and function of the heme chaperone CcmE.” 2003. Doctoral Dissertation, ETH Zürich. Accessed March 05, 2021. http://hdl.handle.net/20.500.11850/147390.

MLA Handbook (7^th Edition):

Enggist, Elisabeth. “The puzzle of cytochrome C biogenesis: structure and function of the heme chaperone CcmE.” 2003. Web. 05 Mar 2021.

Vancouver:

Enggist E. The puzzle of cytochrome C biogenesis: structure and function of the heme chaperone CcmE. [Internet] [Doctoral dissertation]. ETH Zürich; 2003. [cited 2021 Mar 05]. Available from: http://hdl.handle.net/20.500.11850/147390.

Council of Science Editors:

Enggist E. The puzzle of cytochrome C biogenesis: structure and function of the heme chaperone CcmE. [Doctoral Dissertation]. ETH Zürich; 2003. Available from: http://hdl.handle.net/20.500.11850/147390

7. Ester Cristina Borges Araujo. Heme oxigenase-1 na infecção por Toxoplasma gondii: funções divergentes no controle do parasitismo in vitro e in vivo.

Degree: 2011, Federal University of Uberlândia

URL: http://www.bdtd.ufu.br//tde_busca/arquivo.php?codArquivo=3710

►

Toxoplasma gondii é um parasito intracelular obrigatório que induz uma resposta imune do tipo Th1 em seus hospedeiros. O parasito tem uma ampla distribuição mundial,… (more)

▼

Toxoplasma gondii é um parasito intracelular obrigatório que induz uma resposta imune do tipo Th1 em seus hospedeiros. O parasito tem uma ampla distribuição mundial, sendo que as formas mais graves da doença ocorrem principalmente em indivíduos imunocomprometidos. A heme oxigenase-1 (HO-1) é a enzima responsável pelo catabolismo da heme livre, um composto capaz de induzir uma intensa resposta inflamatória. Além disso, a expressão de HO- 1 é induzida diante de vários estímulos, desencadeando uma resposta anti-inflamatória em situações de estresse biológico. Com o objetivo de investigar o papel da HO-1 na infecção por T. gondii, macrófagos RAW 264.7 foram infectados com parasitos da cepa RH e tratados com protoporfirina de zinco IX (ZnPPIX) ou hemina, os quais inibem ou induzem a atividade de HO-1, respectivamente. Para verificação do papel da HO-1 na infecção in vivo, camundongos BALB/c e C57BL/6 foram infectados com a cepa ME49 de T. gondii e tratados com ZnPPIX ou hemina. Os resultados mostraram que a inibição de HO-1 diminuiu o parasitismo nos macrófagos RAW 264.7, sendo que esse mecanismo parece ser independente de óxido nítrico (NO), uma vez que o tratamento com ZnPPIX não alterou os níveis de produção de NO. Além disso, macrófagos infectados, estimulados com IFN-g e tratados com hemina mostraram um aumento na produção de NO. No entanto, essas células quando infectadas e tratadas apenas com hemina apresentaram uma maior replicação do parasito. Durante a infecção in vivo, observou-se que a atividade de HO-1 não ocasionou alterações expressivas na patologia dos órgãos periféricos de camundongos BALB/c e C57BL/6 infectados com T. gondii. Apesar disso, camundongos de ambas as linhagens tratados com ZnPPIX apresentaram maior parasitismo tecidual no pulmão, enquanto que o tratamento com hemina diminuiu a replicação do parasito no intestino e pulmão de camundongos C57BL/6. A mensuração de citocinas (IFN-g, TNF, TGF-b e IL-10) no soro dos animais infectados e tratados com hemina ou ZnPPIX mostrou que a indução ou inibição de HO-1 não altera significativamente os níveis sorológicos de citocinas nos animais BALB/c e C57BL/6 infectados com T. gondii.. Em conclusão, nossos dados sugerem que o aumento da atividade de HO-1 é importante para diminuir a replicação de T. gondii no pulmão e no intestino delgado, embora seja necessária a elucidação dos mecanismos envolvidos. Além disso, os mecanismos mediados pela HO-1 durante a infecção por T. gondii são diferentes in vitro e in vivo, uma vez que o aumento da atividade de HO-1 potencializa a multiplicação do parasito in vitro.

Toxoplasma gondii is an apicomplexan parasite characterized to induce type 1 immune response in infected hosts. The parasite has a worldwide distribution and the more severe forms of the disease occur mainly in immunocompromised individuals. Heme oxygenase-1 (HO-1) is the enzyme that catabolizes free heme that induces an intense inflammatory response. Furthermore, the expression of HO-1 is induced by different stimuli, triggering an anti-inflammatory…

Advisors/Committee Members: Marcelo José Barbosa da Silva, Neide Maria da Silva, Denise Bertolucci Rocha Rodrigues.

Subjects/Keywords: Toxoplasma gondii; BALB/c and C57BL/6 mice; Cytokines; ZnPPIX; IMUNOLOGIA APLICADA; Toxoplasmose; Nitric oxide; Hemin; Camundongos BALB/c e C57BL/6; Citocinas; Heme oxigenase-1; Hemina; Óxido nítrico

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Araujo, E. C. B. (2011). Heme oxigenase-1 na infecção por Toxoplasma gondii: funções divergentes no controle do parasitismo in vitro e in vivo. (Thesis). Federal University of Uberlândia. Retrieved from http://www.bdtd.ufu.br//tde_busca/arquivo.php?codArquivo=3710

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Araujo, Ester Cristina Borges. “Heme oxigenase-1 na infecção por Toxoplasma gondii: funções divergentes no controle do parasitismo in vitro e in vivo.” 2011. Thesis, Federal University of Uberlândia. Accessed March 05, 2021. http://www.bdtd.ufu.br//tde_busca/arquivo.php?codArquivo=3710.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Araujo, Ester Cristina Borges. “Heme oxigenase-1 na infecção por Toxoplasma gondii: funções divergentes no controle do parasitismo in vitro e in vivo.” 2011. Web. 05 Mar 2021.

Vancouver:

Araujo ECB. Heme oxigenase-1 na infecção por Toxoplasma gondii: funções divergentes no controle do parasitismo in vitro e in vivo. [Internet] [Thesis]. Federal University of Uberlândia; 2011. [cited 2021 Mar 05]. Available from: http://www.bdtd.ufu.br//tde_busca/arquivo.php?codArquivo=3710.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Araujo ECB. Heme oxigenase-1 na infecção por Toxoplasma gondii: funções divergentes no controle do parasitismo in vitro e in vivo. [Thesis]. Federal University of Uberlândia; 2011. Available from: http://www.bdtd.ufu.br//tde_busca/arquivo.php?codArquivo=3710

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Aristotle University Of Thessaloniki (AUTH); Αριστοτέλειο Πανεπιστήμιο Θεσσαλονίκης (ΑΠΘ)

8. Georgiou, Sofia. Επίδραση της αίμης στο φλεγμονώδες μικροπεριβάλλον των νεοπλασματικών κυττάρων: αναζήτηση μοριακών στόχων: αναζήτηση μοριακών μηχανισμών σηματοδότησης της ελεύθερης αίμης/αιμίνης και προστασία κυτταροτοξικότητας από θειόλες.

Degree: 2020, Aristotle University Of Thessaloniki (AUTH); Αριστοτέλειο Πανεπιστήμιο Θεσσαλονίκης (ΑΠΘ)

URL: http://hdl.handle.net/10442/hedi/47804

► Heme (iron protoporphyrin IX), as the prosthetic group in several hemoproteins, regulates vital cellular functions in human tissues. However, in hemolytic disorders cytotoxic free heme… (more)

Subjects/Keywords: Κυτταροτοξικότητα επαγώμενη από την ελεύθερη αίμη/αιμίνη; KEAP1/NRF2 σηματοδοτικό μονοπάτι; Ομοιοπολικά σύμπλοκα NAC με αιμίνη; CXC χημειοκίνες; Free heme/hemin-induced cytotoxicity; KEAP1/NRF2 signaling pathway; NAC-hemin adducts; CXC chemokines

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Georgiou, S. (2020). Επίδραση της αίμης στο φλεγμονώδες μικροπεριβάλλον των νεοπλασματικών κυττάρων: αναζήτηση μοριακών στόχων: αναζήτηση μοριακών μηχανισμών σηματοδότησης της ελεύθερης αίμης/αιμίνης και προστασία κυτταροτοξικότητας από θειόλες. (Thesis). Aristotle University Of Thessaloniki (AUTH); Αριστοτέλειο Πανεπιστήμιο Θεσσαλονίκης (ΑΠΘ). Retrieved from http://hdl.handle.net/10442/hedi/47804

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Georgiou, Sofia. “Επίδραση της αίμης στο φλεγμονώδες μικροπεριβάλλον των νεοπλασματικών κυττάρων: αναζήτηση μοριακών στόχων: αναζήτηση μοριακών μηχανισμών σηματοδότησης της ελεύθερης αίμης/αιμίνης και προστασία κυτταροτοξικότητας από θειόλες.” 2020. Thesis, Aristotle University Of Thessaloniki (AUTH); Αριστοτέλειο Πανεπιστήμιο Θεσσαλονίκης (ΑΠΘ). Accessed March 05, 2021. http://hdl.handle.net/10442/hedi/47804.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Georgiou, Sofia. “Επίδραση της αίμης στο φλεγμονώδες μικροπεριβάλλον των νεοπλασματικών κυττάρων: αναζήτηση μοριακών στόχων: αναζήτηση μοριακών μηχανισμών σηματοδότησης της ελεύθερης αίμης/αιμίνης και προστασία κυτταροτοξικότητας από θειόλες.” 2020. Web. 05 Mar 2021.

Vancouver:

Georgiou S. Επίδραση της αίμης στο φλεγμονώδες μικροπεριβάλλον των νεοπλασματικών κυττάρων: αναζήτηση μοριακών στόχων: αναζήτηση μοριακών μηχανισμών σηματοδότησης της ελεύθερης αίμης/αιμίνης και προστασία κυτταροτοξικότητας από θειόλες. [Internet] [Thesis]. Aristotle University Of Thessaloniki (AUTH); Αριστοτέλειο Πανεπιστήμιο Θεσσαλονίκης (ΑΠΘ); 2020. [cited 2021 Mar 05]. Available from: http://hdl.handle.net/10442/hedi/47804.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Georgiou S. Επίδραση της αίμης στο φλεγμονώδες μικροπεριβάλλον των νεοπλασματικών κυττάρων: αναζήτηση μοριακών στόχων: αναζήτηση μοριακών μηχανισμών σηματοδότησης της ελεύθερης αίμης/αιμίνης και προστασία κυτταροτοξικότητας από θειόλες. [Thesis]. Aristotle University Of Thessaloniki (AUTH); Αριστοτέλειο Πανεπιστήμιο Θεσσαλονίκης (ΑΠΘ); 2020. Available from: http://hdl.handle.net/10442/hedi/47804

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

9. Bushnell, Eric Andre. Computational Insights into Redox and Metal Ion Biochemistry.

Degree: PhD, Chemistry and Biochemistry, 2013, National Library of Canada

URL: http://scholar.uwindsor.ca/etd/4915

► Redox reactions are ubiquitous and essential in nature. The enzymes that catalyse these reactions enable the efficient flow of electrons within organisms as well… (more)

Subjects/Keywords: Computational Chemistr; Density Functional Theory; Heme Biochemistry; Iron Biochemistry; Metal-Ion Biochemistry; Redox Catalysis

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Bushnell, E. A. (2013). Computational Insights into Redox and Metal Ion Biochemistry. (Doctoral Dissertation). National Library of Canada. Retrieved from http://scholar.uwindsor.ca/etd/4915

Chicago Manual of Style (16^th Edition):

Bushnell, Eric Andre. “Computational Insights into Redox and Metal Ion Biochemistry.” 2013. Doctoral Dissertation, National Library of Canada. Accessed March 05, 2021. http://scholar.uwindsor.ca/etd/4915.

MLA Handbook (7^th Edition):

Bushnell, Eric Andre. “Computational Insights into Redox and Metal Ion Biochemistry.” 2013. Web. 05 Mar 2021.

Vancouver:

Bushnell EA. Computational Insights into Redox and Metal Ion Biochemistry. [Internet] [Doctoral dissertation]. National Library of Canada; 2013. [cited 2021 Mar 05]. Available from: http://scholar.uwindsor.ca/etd/4915.

Council of Science Editors:

Bushnell EA. Computational Insights into Redox and Metal Ion Biochemistry. [Doctoral Dissertation]. National Library of Canada; 2013. Available from: http://scholar.uwindsor.ca/etd/4915

University of California – Irvine

10. Chao, Alex. Characterization of a Heme Degrading Enzyme from Mycobacterium tuberculosis.

Degree: Biological Sciences, 2018, University of California – Irvine

URL: http://www.escholarship.org/uc/item/8vk0723j

► Iron is important for pathogen survival and pathogens such as Mycobacterium tuberculosis (Mtb) have evolved pathways to acquire host iron. One such mechanism Mtb has… (more)

▼ Iron is important for pathogen survival and pathogens such as Mycobacterium tuberculosis (Mtb) have evolved pathways to acquire host iron. One such mechanism Mtb has evolved is the acquisition of heme, where Mtb imports host heme for degradation and iron release. In the cytosol, the heme degrading enzyme MhuD is responsible for the cleavage of heme and the liberation iron for use by Mtb. In this work we document our ongoing efforts to better understand MhuD and its larger role in Mtb. Although the structure of the inactive diheme form of MhuD was previously determined, the structure of its active monoheme form was unresolved. We were able to determine the crystal structure of the cyano-derivative of MhuD-monoheme to obtain insights into MhuD heme degradation and product uniqueness. Heme ruffling, proposed to be responsible for heme’s reactivity within the active site of MhuD homologs, was observed in the MhuD-monoheme structure. Mutations to apparent heme ruffling residues Phe23 and Trp66 appear to abolish MhuD’s heme degradation activity suggesting the importance of heme ruffling in MhuD activity. Residues were also identified potentially responsible for MhuD’s unique degradation products. We found that mutation of one such residue, Arg26 into a serine, alters MhuD’s heme degradation into biliverdin and formaldehyde. Efforts to biophysically and structurally characterize the MhuD R26S mutant suggests that there is a reduction in heme ruffling in the mutant which may lead to the altered degradation product. We also explored the role MhuD plays in the pharmacological inhibition of Mtb growth of mice infected with Mtb by the heme analog tin-protoporphrin IX (SnPPIX). Despite its ability to inhibit the human heme degrader, heme oxygenase, SnPPIX did not appear to inhibit MhuD’s ability to degrade heme. Lastly, we also carried out preliminary research towards the identification of a MhuD electron donor as well as of a potential protein partner for MhuD product release. To date, neither proposed MhuD interaction partners have been identified, however more candidate proteins remain to be purified and tested.

Subjects/Keywords: Biochemistry; Heme; Metal Ion Binding; Mycobacterium tuberculosis; Oxygenase

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APA (6^th Edition):

Chao, A. (2018). Characterization of a Heme Degrading Enzyme from Mycobacterium tuberculosis. (Thesis). University of California – Irvine. Retrieved from http://www.escholarship.org/uc/item/8vk0723j

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Chao, Alex. “Characterization of a Heme Degrading Enzyme from Mycobacterium tuberculosis.” 2018. Thesis, University of California – Irvine. Accessed March 05, 2021. http://www.escholarship.org/uc/item/8vk0723j.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Chao, Alex. “Characterization of a Heme Degrading Enzyme from Mycobacterium tuberculosis.” 2018. Web. 05 Mar 2021.

Vancouver:

Chao A. Characterization of a Heme Degrading Enzyme from Mycobacterium tuberculosis. [Internet] [Thesis]. University of California – Irvine; 2018. [cited 2021 Mar 05]. Available from: http://www.escholarship.org/uc/item/8vk0723j.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Chao A. Characterization of a Heme Degrading Enzyme from Mycobacterium tuberculosis. [Thesis]. University of California – Irvine; 2018. Available from: http://www.escholarship.org/uc/item/8vk0723j

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Notre Dame

11. Richard Charles Kurker, Jr. Beyond O₂: Biochemistry of Chlorite Dismutases from Klebsiella and Staphylococcus</h1>.

Degree: Chemistry and Biochemistry, 2013, University of Notre Dame

URL: https://curate.nd.edu/show/2b88qc00g2m

► This thesis examines the relationships among members of the chlorite dismutase (Cld) heme protein family, focusing on sequence, structural, and functional characterization of two… (more)

▼ This thesis examines the relationships among members of the chlorite dismutase (Cld) heme protein family, focusing on sequence, structural, and functional characterization of two highly distinct chlorite dismutases from divergent phyla. The name “chlorite dismutase” refers to the heme-facilitated conversion of chlorite (ClO2-) to chloride (Cl-) and O2, a remarkable reaction in that Cld is the only well-characterized enzyme, aside from photosystem II, capable of O-O bond generation. The Cld from Dechloromonas aromatica (DaCld) is a homopentamer that very rapidly and efficiently generates oxygen from chlorite. Interestingly, Cld homologues are found among 10 diverse phyla, suggesting ancient origins for the family. The handful of Clds from known perchlorate respirers group closely in protein-based phylogenetic analysis, which could be indicative of an evolutionary response to a relatively recent pollutant, chlorite. The majority of Clds are not expected to respire perchlorate, leaving a vast amount of relevant bacterial genome unexplored with respect to gene product function. In order to explore Cld diversity, Cld homolog proteins from the Gram-positive Firmicutes Staphylococcus aureus (Sa) and the Gram-negative Proteobacterium Klebsiella pneumoniae (Kp), two very different types of bacteria, were functionally characterized. Both Sa and Kp ESKAPE pathogens, drug-resistant bacteria that increasingly escape the effect of antibiotics and account for about 2/3 of all hospital-acquired infections, so gene product characterization for these particular bacteria has the potential for eventual organism-specific antimicrobial applications. The active site of KpCld very closely resembles that of DaCld but the protein is a dimer, while SaCld is a homopentamer like DaCld but lacks the distal Arg critical for the Cld reaction. These two proteins were expressed, purified with bound heme, and studied through a wide array of bioinformatics and biochemical techniques. Furthermore, their corresponding gene knockouts were constructed and their phenotypes studied in parallel. Bioinformatic, biochemical, and genetic studies showed that SaCld, or SaHemQ, lacks Cld activity, instead playing a critical role in the heme biosynthesis pathway, particularly in the final few steps. Knockout growth curves, metabolite analyses, and reactivity studies, among others, provided evidence that SaCld is likely not a direct enzyme in the pathway, but rather serves as an iron, heme, or redox sensor that is able to influence the collaborative activity of protoporphyrinogen oxidase and ferrochelatase, the final two enzymes in the heme biosynthetic pathway. In stark contrast to this functionality is KpCld, a protein that performs the Cld reaction despite lacking both a perchlorate reductase and a biological need by the organism to metabolize perchorate. Instead, KpCld has been shown to be capable of reductant oxidation (specifically, ABTS) and chlorination upon chlorite addition, and the Cld reaction can be controlled by the presence (or absence) of O2 as… Advisors/Committee Members: Dr. Amanda Hummon, Committee Member, Dr. Jennifer DuBois, Committee Co-Chair, Dr. Anthony Serianni, Committee Member, Dr. Paul Huber, Committee Co-Chair.

Subjects/Keywords: peroxidase; chlorite dismutase; protein biochemistry; bioinformatics; heme biosynthesis; catalase

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APA (6^th Edition):

Richard Charles Kurker, J. (2013). Beyond O₂: Biochemistry of Chlorite Dismutases from Klebsiella and Staphylococcus</h1>. (Thesis). University of Notre Dame. Retrieved from https://curate.nd.edu/show/2b88qc00g2m

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Richard Charles Kurker, Jr. “Beyond O₂: Biochemistry of Chlorite Dismutases from Klebsiella and Staphylococcus</h1>.” 2013. Thesis, University of Notre Dame. Accessed March 05, 2021. https://curate.nd.edu/show/2b88qc00g2m.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Richard Charles Kurker, Jr. “Beyond O₂: Biochemistry of Chlorite Dismutases from Klebsiella and Staphylococcus</h1>.” 2013. Web. 05 Mar 2021.

Vancouver:

Richard Charles Kurker J. Beyond O₂: Biochemistry of Chlorite Dismutases from Klebsiella and Staphylococcus</h1>. [Internet] [Thesis]. University of Notre Dame; 2013. [cited 2021 Mar 05]. Available from: https://curate.nd.edu/show/2b88qc00g2m.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Richard Charles Kurker J. Beyond O₂: Biochemistry of Chlorite Dismutases from Klebsiella and Staphylococcus</h1>. [Thesis]. University of Notre Dame; 2013. Available from: https://curate.nd.edu/show/2b88qc00g2m

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of Maryland

12. Connor, Katherine Lindsey. Discovery, Characterization and Mechanistic Study of a Novel L-Tyrosine Hydroxylase in the Biosynthesis of Anthramycin.

Degree: Biochemistry, 2012, University of Maryland

URL: http://hdl.handle.net/1903/13207

► A tyrosine hydroxylase coded by orf13 of the anthramycin biosynthesis gene cluster is proposed to catalyze the ortho-hydroxylation of L-tyrosine to L-DOPA as the initial… (more)

Subjects/Keywords: Biochemistry; anthramycin; aromatic hydroxylation; heme peroxidase; pyrrolo[1,4]benzodiazepine; tyrosine hydroxylase

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APA (6^th Edition):

Connor, K. L. (2012). Discovery, Characterization and Mechanistic Study of a Novel L-Tyrosine Hydroxylase in the Biosynthesis of Anthramycin. (Thesis). University of Maryland. Retrieved from http://hdl.handle.net/1903/13207

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Connor, Katherine Lindsey. “Discovery, Characterization and Mechanistic Study of a Novel L-Tyrosine Hydroxylase in the Biosynthesis of Anthramycin.” 2012. Thesis, University of Maryland. Accessed March 05, 2021. http://hdl.handle.net/1903/13207.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Connor, Katherine Lindsey. “Discovery, Characterization and Mechanistic Study of a Novel L-Tyrosine Hydroxylase in the Biosynthesis of Anthramycin.” 2012. Web. 05 Mar 2021.

Vancouver:

Connor KL. Discovery, Characterization and Mechanistic Study of a Novel L-Tyrosine Hydroxylase in the Biosynthesis of Anthramycin. [Internet] [Thesis]. University of Maryland; 2012. [cited 2021 Mar 05]. Available from: http://hdl.handle.net/1903/13207.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Connor KL. Discovery, Characterization and Mechanistic Study of a Novel L-Tyrosine Hydroxylase in the Biosynthesis of Anthramycin. [Thesis]. University of Maryland; 2012. Available from: http://hdl.handle.net/1903/13207

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

13. Parthasarathy, Sudharsan. Evolutionary divergence in proteins: experimental and theoretical studies on the stability and electrochemical properties of cytochrome b5.

Degree: PhD, Biochemistry & Molecular Biology, 2012, University of Kansas

URL: http://hdl.handle.net/1808/10298

► Cytochrome b5 (CYB5) is a small ubiquitous heme binding protein whose biochemical function is electron transfer. Two isoforms of CYB5 are found in mammals, which… (more)

▼ Cytochrome b5 (CYB5) is a small ubiquitous heme binding protein whose biochemical function is electron transfer. Two isoforms of CYB5 are found in mammals, which are named based on their specific subcellular localization. One isoform is localized to the outer membrane of mitochondria (OMb5) and the other isoform is localized to the endoplasmic reticulum (Mcb5). Available evidence indicates that Mc and OM b5 isoforms arose from a gene duplication event that led to functional divergence. High sequence identity is observed when comparing individual isoforms across mammalian organisms. A highly conserved protein fold is also a feature when comparing the two isoforms. However the two isoforms differ remarkably with respect to their biophysical and biochemical properties. This dissertation focusses on analyzing the specific differences in Mc and OMb5 amino acid sequences that translate into subtle differences in structure, and to correlate them with differences in the biophysical properties of the two isoforms. A combination of experimental and theoretical methods has been used in order to study the differences between Mcb5 and Omb5. In chapter 3, I describe the X-ray crystal structures of the rat Omb5 (rOMb5) and human Omb5 (hOMb5), which reveal a striking difference in structure due to a difference in buried residue 21. The presence of Leu at position 21 in hOMb5 causes a displacement of the first two residues in beta 5, and consequent loss of two of the three hydrogen bonds between beta 5 and beta 4. Hydrogen bonding between the residues is instead mediated by two well ordered, fully buried water molecules. MD simulations of the hOMb5 protein, with and without the water molecules, provided mechanistic insight into the similarity in biophysical properties between hOMb5 and rOMb5. This study also provided information on the versatility of the CYB5 fold to resist internal mutations. Chapter 4 is a mutation based study that attempts to combine the most stabilizing features of OMb5 and Mcb5. The model proteins used here are rOMb5 and the bovine Mcb5 (bMcb5). We performed a systematic incorporation of amino acids from rOMb5 into the corresponding positions in bMcb5 which culminated in generating a hybrid protein (hybb5) that combined the most stabilizing features of the two proteins. We were successful in generating a series of mutants of increasing stability that altered both heme binding strength and apo protein stability. Further investigation revealed that rOMb5 displayed greater stability on account of the amino acid at position 71 (Leu). The presence of Leu in OMb5 isoforms results in generation of a more compact empty heme binding pocket that plays a major part in stabilizing OMb5 in contrast to Mcb5 isoforms which contain a more polar residue (Ser) at position 71. Chapter 5 utilizes the mutants generated as part of the study in chapter 4 to understand the factors responsible for modulating the redox potential difference in Omb5 and Mcb5. The initial part of the chapter focusses on measurement of redox potentials of… Advisors/Committee Members: Kuczera, Krzysztof (advisor), Benson, David R (cmtemember), Richter, Mark (cmtemember), Lamb, Audrey (cmtemember), Zhu, Hao (cmtemember).

Subjects/Keywords: Biochemistry; Biophysics; Cytochrome b5; Heme; Molecular dynamics; Redox potential

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APA (6^th Edition):

Parthasarathy, S. (2012). Evolutionary divergence in proteins: experimental and theoretical studies on the stability and electrochemical properties of cytochrome b5. (Doctoral Dissertation). University of Kansas. Retrieved from http://hdl.handle.net/1808/10298

Chicago Manual of Style (16^th Edition):

Parthasarathy, Sudharsan. “Evolutionary divergence in proteins: experimental and theoretical studies on the stability and electrochemical properties of cytochrome b5.” 2012. Doctoral Dissertation, University of Kansas. Accessed March 05, 2021. http://hdl.handle.net/1808/10298.

MLA Handbook (7^th Edition):

Parthasarathy, Sudharsan. “Evolutionary divergence in proteins: experimental and theoretical studies on the stability and electrochemical properties of cytochrome b5.” 2012. Web. 05 Mar 2021.

Vancouver:

Parthasarathy S. Evolutionary divergence in proteins: experimental and theoretical studies on the stability and electrochemical properties of cytochrome b5. [Internet] [Doctoral dissertation]. University of Kansas; 2012. [cited 2021 Mar 05]. Available from: http://hdl.handle.net/1808/10298.

Council of Science Editors:

Parthasarathy S. Evolutionary divergence in proteins: experimental and theoretical studies on the stability and electrochemical properties of cytochrome b5. [Doctoral Dissertation]. University of Kansas; 2012. Available from: http://hdl.handle.net/1808/10298

University of Pennsylvania

14. Auman, Dirk. Uncovering Biophysical Determinants Of Oxidoreductase Function Through De Novo Protein Design.

Degree: 2019, University of Pennsylvania

URL: https://repository.upenn.edu/edissertations/3521

► Oxidoreductases are a diverse class of enzymes defined by their chemical role of transferring electrons from one substrate to another. Comprising the functional cores of… (more)

▼ Oxidoreductases are a diverse class of enzymes defined by their chemical role of transferring electrons from one substrate to another. Comprising the functional cores of photosynthetic, chemosynthetic, and cellular respiratory machinery, “redox proteins” and the catalysis they enable form the foundation biological energy transduction. Mastering the mechanisms by which these enzymes work is the key to understanding how life works and drives the improvement of an as of yet poorly developed theoretical framework for describing the multiscale chemistry and physics crucial to future developments in synthetic biology, mesoscale engineering, and macromolecular catalysis. Redox proteins are characterized by their near universal incorporation of one or more cofactors, non-protein molecules with notable electrochemical and/or photophysical properties that play a fundamental role in the enzyme’s behavior. The functions of these enzymes can then be thought of as having two aspects: the cofactor(s), whose physical chemistry dictates the general mechanism of energy transduction, and the protein scaffold, which via microenvironment, relative positioning, geometric strain, and other mechanical properties modulate the energetic landscape and gate the influx and efflux of reactants and products. Separation of these aspects in practice, however, is often hindered by the sheer structural complexity of the natural machinery in question, even the simpler ones. Billions of years of evolution can incorporate many inessential elements, creating what is known as irreducible Mullerian complexity. Observational studies are useful but have their fundamental limitations. True validation of understanding comes through construction and functional verification. In accordance with this philosophy, we set out to recreate two representative redox chemistries in minimally designed model protein scaffolds to establish the basic requirements for their respective catalytic processes. Specifically, we focus on the suppression of heme-based superoxide formation and the promotion of photo-induced flavin activation in two classes of four-helix bundle proteins with complementary biophysical properties. This thesis discusses the implementation of both active sites in each of the two classes of scaffolds, and draws conclusions about the essential components of each. With the long-term goals of engineerability and biological integration in mind, we also demonstrate the ability of these model scaffolds to interface with two types of natural membrane transport complexes. In addition, we show that the 4-helical bundle domain retains functional independence even as a polymer of up to 16 alpha helices. The thesis ends with a discussion on the present limits and future potential of minimal models and protein engineering as a whole.

Subjects/Keywords: flavin; heme; magnetic sensing; oxygen; protein engineering; transport; Biochemistry; Biophysics

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APA (6^th Edition):

Auman, D. (2019). Uncovering Biophysical Determinants Of Oxidoreductase Function Through De Novo Protein Design. (Thesis). University of Pennsylvania. Retrieved from https://repository.upenn.edu/edissertations/3521

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Auman, Dirk. “Uncovering Biophysical Determinants Of Oxidoreductase Function Through De Novo Protein Design.” 2019. Thesis, University of Pennsylvania. Accessed March 05, 2021. https://repository.upenn.edu/edissertations/3521.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Auman, Dirk. “Uncovering Biophysical Determinants Of Oxidoreductase Function Through De Novo Protein Design.” 2019. Web. 05 Mar 2021.

Vancouver:

Auman D. Uncovering Biophysical Determinants Of Oxidoreductase Function Through De Novo Protein Design. [Internet] [Thesis]. University of Pennsylvania; 2019. [cited 2021 Mar 05]. Available from: https://repository.upenn.edu/edissertations/3521.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Auman D. Uncovering Biophysical Determinants Of Oxidoreductase Function Through De Novo Protein Design. [Thesis]. University of Pennsylvania; 2019. Available from: https://repository.upenn.edu/edissertations/3521

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Florida International University

15. Butcher, David S. Thermodynamics and Kinetics of Ligand Photodissociation in Heme Proteins and Formation of DNA i-Motif.

Degree: PhD, Chemistry, 2017, Florida International University

URL: https://digitalcommons.fiu.edu/etd/3259 ; 10.25148/etd.FIDC001737 ; FIDC001737

► Heme proteins carry out a diverse array of functions in vivo while maintaining a well-conserved 3-over-3 α-helical structure. Human hemoglobin (Hb) is well-known for… (more)

▼ Heme proteins carry out a diverse array of functions in vivo while maintaining a well-conserved 3-over-3 α-helical structure. Human hemoglobin (Hb) is well-known for its oxygen transport function. Type 1 non-symbiotic hemoglobins (nsHb1) in plants and bacterial flavohemoglobins (fHb) from a variety of bacterial species have been predicted to carry out a nitric oxide dioxygenase function. In nsHb1 and fHb this function has been linked to protection from nitrosative stress. Herein, I combine photoacoustic calorimetry (PAC), transient absorption spectroscopy (TA), and classical molecular dynamics (cMD) simulations to characterize molecular mechanism of diatomic ligand interactions with a hexa-coordinate globin from plant (rice hemoglobin), bacterial flavohemoglobins and human hemoglobin. In rice type 1 non-symbiotic hemoglobin (rHb1), the dynamics and energetics of structural changes associated with ligand photodissociation is strongly impacted by solvent and temperature, namely CO escape from the protein matrix is slower at pH = 6.0 compare to neutral pH (ns) due to the CD loop reorganization which forms a pathway for ligand escape. In human hemoglobin, exogenous allosteric effectors modulate energetics of conformational changes associated with the CO and O₂ escape although the effectors impact on rate constants for ligand association is small. The conformational dynamics associated with ligand photorelease from fHbs from Cupriavidus necator (FHP) and Staphylococcus aureus (HMP_Sa) are strongly modulated by the presence of azole drugs indicating that drug association modulates structural properties of the heme binding pocket. In addition, we carried out a study of the formation of the DNA intercalated motif (i-motif). The formation of the structure is strongly favored at acidic pH; therefore, PAC was combined with a 2-nitrobenzaldehyde pH-jump to probe formation of the i-motif on fast timescales. i-Motif folding is two-step process with the initial protonation of cytosine residues being endothermic with ΔH_fast=8.5 ± 7.0 kcal mol^-1 and ΔV_fast=10.4 ± 1.6 mL mol^-1 and subsequent nucleation/i-motif folding (τ = 140 ns) with ΔH_slow=-51.5 ± 4.8 kcal mol^-1 and ΔV_slow=-6.6 ± 0.9 mL mol^-1. The above results indicate that PAC can be employed to study diverse biochemical reactions such as DNA folding, drug binding and ligand photorelease from proteins. Advisors/Committee Members: Jaroslava Miksovska, Konstantinos Kavallieratos, Yuk-Ching Tse-Dinh, Irina Agoulnik, Joong Ho Moon.

Subjects/Keywords: heme; heme protein; hemoglobin; photoacoustic; photoacoustic calorimetry; biophysical chemistry; i-motif; flavohemoglobin; non-symbiotic; Biochemistry; Biophysics

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APA (6^th Edition):

Butcher, D. S. (2017). Thermodynamics and Kinetics of Ligand Photodissociation in Heme Proteins and Formation of DNA i-Motif. (Doctoral Dissertation). Florida International University. Retrieved from https://digitalcommons.fiu.edu/etd/3259 ; 10.25148/etd.FIDC001737 ; FIDC001737

Chicago Manual of Style (16^th Edition):

Butcher, David S. “Thermodynamics and Kinetics of Ligand Photodissociation in Heme Proteins and Formation of DNA i-Motif.” 2017. Doctoral Dissertation, Florida International University. Accessed March 05, 2021. https://digitalcommons.fiu.edu/etd/3259 ; 10.25148/etd.FIDC001737 ; FIDC001737.

MLA Handbook (7^th Edition):

Butcher, David S. “Thermodynamics and Kinetics of Ligand Photodissociation in Heme Proteins and Formation of DNA i-Motif.” 2017. Web. 05 Mar 2021.

Vancouver:

Butcher DS. Thermodynamics and Kinetics of Ligand Photodissociation in Heme Proteins and Formation of DNA i-Motif. [Internet] [Doctoral dissertation]. Florida International University; 2017. [cited 2021 Mar 05]. Available from: https://digitalcommons.fiu.edu/etd/3259 ; 10.25148/etd.FIDC001737 ; FIDC001737.

Council of Science Editors:

Butcher DS. Thermodynamics and Kinetics of Ligand Photodissociation in Heme Proteins and Formation of DNA i-Motif. [Doctoral Dissertation]. Florida International University; 2017. Available from: https://digitalcommons.fiu.edu/etd/3259 ; 10.25148/etd.FIDC001737 ; FIDC001737

16. Russell, Nicholas H. Heme Oxygenase 1 expression after traumatic brain injury and effect of pharmacological manipulation on functional recovery.

Degree: PhD, Neuroscience, 2017, Virginia Commonwealth University

URL: https://doi.org/10.25772/D2K0-MM59 ; https://scholarscompass.vcu.edu/etd/5525

► Traumatic Brain Injury (TBI) is an increasingly diagnosed constellation of injuries derived from acute mechanical trauma to the brain. With the rise of advanced… (more)

▼ Traumatic Brain Injury (TBI) is an increasingly diagnosed constellation of injuries derived from acute mechanical trauma to the brain. With the rise of advanced neuroimaging techniques recent focus has oriented primarily towards the mild-moderate range of TBI which previously was missed diagnostically. Characteristically, these advances have shown increasing areas of micro-hemorrhage in susceptible areas of the brain and to date there are no treatment modalities targeting micro-hemorrhages or their sequelae. This dissertation explores the effects of the resulting heme processing response in the days following injury with a particular focus on inducing early heme clearance from the parenchyma using a rat central fluid percussion injury model in the mild-moderate injury range. Since heme is released ~24-48 hours post-injury and is known to be cytotoxic we observed there may be a critical window for treatment to clear heme before it is spontaneously released and to increase the buffering capacity of the tissue. We targeted heme clearance by using drugs known to increased expression of Nrf2, an upstream transcriptional regulator of the canonical heme processing protein heme oxygenase 1 (HO-1), and tracking expression of HO-1, the iron sequestration/storage proteins Lipocalin 2 (LCN2) and Ferritin (FTL), as well as the activity of matrix metalloproteinases 2 and 9 (MMP2, MMP9). We examined both tissue known to be frankly hemorrhagic (the neocortex) as well as tissue lacking any identifiable bleed (the hippocampus). We demonstrated that using the HO-1 inducers Hemin and Sulforaphane in a single dose paradigm given 1 hour post-injury heme clearance was accelerated in the neocortex with the majority of heme pigment processed by 24 hours post-injury. Further there was significant attenuation of protein expression in HO-1 and ferritin as well as the enzyme activity of MMP2 and MMP9 in both the neocortex and the hippocampus. Behavioral attenuation was also seen in both rotarod and Morris water maze tests. While we intended to target hemorrhagic processing after injury, and indeed demonstrated improved clearance of heme from post-injury hemorrhagic regions of the brain, in both tissues studied we observed remarkably similar responses to the drugs utilized in protein expression, enzyme activity, and behavioral improvement which may suggest a globally improved pathologic state or that there are unidentified pathologic micro-hemorrhages or leaky vessels which extend further into the brain parenchyma than currently identified. Advisors/Committee Members: Linda L. Phillips, Clive M. Baumgarten, Andrew K. Ottens, John T. Povlishock, Dong Sun.

Subjects/Keywords: Traumatic Brain Injury; TBI; Heme Oxygenase 1; HO-1; Hemin; Sulforaphane; Medical Neurobiology

…176 2.9.3 Correlated Post-injury changes in heme processing pathway molecules… …217 3.5 Heme Pigment Disappearance in Drug Treated Animals… …218 3.5.1 Figure 3-4: Heme Procesing Cartoon… …220 3.5.2 Figure 3-5: Loss of Heme Pigment After Drug Treatment 1d Post-Injury… …325 4.2 Post-Injury Heme Processing…

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APA (6^th Edition):

Russell, N. H. (2017). Heme Oxygenase 1 expression after traumatic brain injury and effect of pharmacological manipulation on functional recovery. (Doctoral Dissertation). Virginia Commonwealth University. Retrieved from https://doi.org/10.25772/D2K0-MM59 ; https://scholarscompass.vcu.edu/etd/5525

Chicago Manual of Style (16^th Edition):

Russell, Nicholas H. “Heme Oxygenase 1 expression after traumatic brain injury and effect of pharmacological manipulation on functional recovery.” 2017. Doctoral Dissertation, Virginia Commonwealth University. Accessed March 05, 2021. https://doi.org/10.25772/D2K0-MM59 ; https://scholarscompass.vcu.edu/etd/5525.

MLA Handbook (7^th Edition):

Russell, Nicholas H. “Heme Oxygenase 1 expression after traumatic brain injury and effect of pharmacological manipulation on functional recovery.” 2017. Web. 05 Mar 2021.

Vancouver:

Russell NH. Heme Oxygenase 1 expression after traumatic brain injury and effect of pharmacological manipulation on functional recovery. [Internet] [Doctoral dissertation]. Virginia Commonwealth University; 2017. [cited 2021 Mar 05]. Available from: https://doi.org/10.25772/D2K0-MM59 ; https://scholarscompass.vcu.edu/etd/5525.

Council of Science Editors:

Russell NH. Heme Oxygenase 1 expression after traumatic brain injury and effect of pharmacological manipulation on functional recovery. [Doctoral Dissertation]. Virginia Commonwealth University; 2017. Available from: https://doi.org/10.25772/D2K0-MM59 ; https://scholarscompass.vcu.edu/etd/5525

17. Campbell, James H. Effect of hemin and baicalein on heme oxygenase-1 accumulation and function in Xenopus laevis cultured cells.

Degree: 2018, University of Waterloo

URL: http://hdl.handle.net/10012/13180

► Heme oxygenase-1 (HO-1) is a stress-inducible enzyme that catalyzes the rate-limiting step in the hemin degradation pathway. Studies in mammalian systems determined that HO-1 promoted… (more)

▼ Heme oxygenase-1 (HO-1) is a stress-inducible enzyme that catalyzes the rate-limiting step in the hemin degradation pathway. Studies in mammalian systems determined that HO-1 promoted cell survival by reducing oxidative damage in cells exposed to heavy metal toxicants. While most of the knowledge regarding HO-1 synthesis and function was derived from mammals, less is known about this stress-inducible protein in poikilothermic vertebrates such as amphibians and fish. The aim of the present study is to investigate stress-induced accumulation of HO-1 and its potential cytoprotective effects in A6 kidney epithelial cells derived from the aquatic frog, Xenopus laevis. Treatment of A6 cells with hemin, baicalein (a plant flavinoid) or CdCl2 induced HO-1 accumulation in a concentration- and time-dependent manner. While CdCl2 treatment also induced the accumulation of the heat shock proteins (HSPs), HSP70 and HSP30, their accumulation was not detectable in cells treated with baicalein or hemin. Immunocytochemical analysis revealed that hemin, baicalein and CdCl2 treatment induced the accumulation of HO-1 primarily in the perinuclear region in a granular pattern with some localization in the nucleus. While treatment of cells with 25 μM hemin or 200 μM baicalein induced slight disorganization of actin filaments, exposure of cells to higher concentrations of CdCl2 (e.g. 200 μM) produced pronounced actin cytoskeletal disorganization and membrane ruffling. Stress-induced accumulation of HO-1 was the result of de novo synthesis since upregulated HO-1 levels were inhibited by the transcriptional and translational inhibitors, actinomycin D and cycloheximide, respectively. Furthermore, the heat shock factor 1 (HSF1) inhibitor, KNK437, suppressed hemin-, baicalein-, and CdCl2-induced HO-1 accumulation. Since previous studies reported that stress-induced HO-1 accumulation may be associated with oxidative stress, the levels of the ROS-responsive transcription factor, Nrf2, were measured and found to increase in cells treated with baicalein and CdCl2 but not with hemin. However, levels of the antioxidant enzyme, peroxiredoxin 5 (PRDX5), were elevated in response to all three stressors. Finally, analysis of reactive oxygen species (ROS) production using a fluorescent probe detected enhanced ROS amounts in A6 cells treated with baicalein and CdCl2 but not with hemin. In another approach, A6 cells, which were incubated with buthionine sulfoximine (BSO), an inhibitor of glutathione synthesis and a known inducer of ROS, enhanced HO1 accumulation in cells treated with CdCl2 but with either hemin or baicalein. This study also determined that HO-1 accumulation was required for cytoprotection of A6 cells to CdCl2 since cotreatment with the HO-1 enzyme activity inhibitors, tin protoporphyrin (SnPP) and zinc protoporphyrin (ZnPP), enhanced cadmium-induced actin cytoskeleton dysregulation and the formation of aggregated protein and aggresome-like structures. Finally, this study examined whether treatment of A6 cells with hemin or baicalein could…

Subjects/Keywords: HO-1; Heme oxygenase; Cadmium; Aggregated Protein; Aggresomes; HSP70; HSP30; Xenopus; Immunocytochemistry; Cytoskeleton; Hemin; Baicalein

…Henrietta Lacks heme chloride 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid Hemin… …3.0 Results 3.1 Characterization of the heme oxygenase-1 (HO-1) amino acid… …sequence in X. laevis 3.2 Pattern of HO-1 accumulation in cells treated with hemin, baicalein or… …tubulin cytoskeletal structure in hemin-, baicalein- and CdCl2treated cells. 3.4. Effect of… …transcriptional and translational inhibitors on hemin- and baicalein-induced HO-1 accumulation. 3.5…

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APA (6^th Edition):

Campbell, J. H. (2018). Effect of hemin and baicalein on heme oxygenase-1 accumulation and function in Xenopus laevis cultured cells. (Thesis). University of Waterloo. Retrieved from http://hdl.handle.net/10012/13180

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Campbell, James H. “Effect of hemin and baicalein on heme oxygenase-1 accumulation and function in Xenopus laevis cultured cells.” 2018. Thesis, University of Waterloo. Accessed March 05, 2021. http://hdl.handle.net/10012/13180.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Campbell, James H. “Effect of hemin and baicalein on heme oxygenase-1 accumulation and function in Xenopus laevis cultured cells.” 2018. Web. 05 Mar 2021.

Vancouver:

Campbell JH. Effect of hemin and baicalein on heme oxygenase-1 accumulation and function in Xenopus laevis cultured cells. [Internet] [Thesis]. University of Waterloo; 2018. [cited 2021 Mar 05]. Available from: http://hdl.handle.net/10012/13180.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Campbell JH. Effect of hemin and baicalein on heme oxygenase-1 accumulation and function in Xenopus laevis cultured cells. [Thesis]. University of Waterloo; 2018. Available from: http://hdl.handle.net/10012/13180

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

18. Quick-Cleveland, Jen. Primary microRNA processing in humans: biology, biotechnology and disease.

Degree: Biological Chemistry, 2017, UCLA

URL: http://www.escholarship.org/uc/item/4sh028f3

► MicroRNAs (miRNAs) are a class of non-coding RNAs that tune gene expression by negatively regulating at least 60% of protein-coding genes. In animals, they are… (more)

▼ MicroRNAs (miRNAs) are a class of non-coding RNAs that tune gene expression by negatively regulating at least 60% of protein-coding genes. In animals, they are required for development and cell physiology. Due to their role in controlling gene expression, dysregulation of miRNA biogenesis can cause genetic disorders, immunity deficits, neurological problems, and cancers. miRNA genes are transcribed into primary miRNA (pri-miRNAs), which undergo a multi-step maturation process. The first step occurs in the nucleus, where the pri-miRNA is cleaved by the Microprocessor Complex (MC). The MC contains the ribonuclease Drosha and an RNA-binding hemoprotein DGCR8. The MC specifically recognizes the characteristic pri-miRNA hairpin to initiate miRNA maturation. This thesis centers on the nuclear step of miRNA biogenesis. My research has two main areas of focus; 1) dissecting the molecular and structural determinants that govern pri-miRNA processing, and 2) investigating the regulation of pri-miRNA processing in normal physiology and diseases.The MC identifies pri-miRNA substrates from a myriad of other RNAs. DGCR8 plays an important role in pri-miRNA recognition, but the mechanism was unknown. DGRC8 contains two double-stranded RNA-binding domains (dsRBDs), but these domains do not provide specificity. It has been shown that “junctions” between single-stranded and double-stranded regions in pri-miRNAs are important features that define MC substrates. However, the protein moiety that recognizes pri-miRNA junctions had not been identified. We discovered that DGCR8 contains an RNA-binding heme domain (Rhed) that directly and specifically binds pri-miRNA junctions. Further, we showed that the Rhed and its RNA-binding surface are required for efficient pri-miRNA processing.Previous studies of our lab showed that the pri-miRNA processing activity of DGCR8 specifically requires heme in its Fe(III) redox state. However, it is unknown how much Fe(III) heme is available in cells and how much is required to support pri-miRNA processing. During our investigation of the Rhed-pri-miRNA interface, we performed mutagenesis on DGCR8 that led to identification of single mutations with reduced heme affinity but nearly full processing activity in cells. This meant that the Fe(III) heme affinities of these mutants are sufficient for them to acquire heme and to process pri-miRNAs. In contrast, all heme-binding-deficient mutants of DGCR8 we previously characterized are inactive in cells and have lower affinities for Fe(III) heme. We discovered that the Fe(III) heme affinity threshold for activating DGCR8 is shifted by overall heme availability changes in cells. These results indicate the presence of an available ferric heme pool that distinctly determines pri-miRNA processing efficiency in cells. Our study suggests cellular redox state and currently unknown Fe(III) heme-specific transporter proteins may be important for regulating miRNA maturation. Secondary structure is a defining characteristic of pri-miRNA substrates. Substantial effort has been…

Subjects/Keywords: Molecular biology; Biochemistry; DGCR8; Fe(III) heme; microRNA; miRNA and cancer; shRNA

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APA (6^th Edition):

Quick-Cleveland, J. (2017). Primary microRNA processing in humans: biology, biotechnology and disease. (Thesis). UCLA. Retrieved from http://www.escholarship.org/uc/item/4sh028f3

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Quick-Cleveland, Jen. “Primary microRNA processing in humans: biology, biotechnology and disease.” 2017. Thesis, UCLA. Accessed March 05, 2021. http://www.escholarship.org/uc/item/4sh028f3.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Quick-Cleveland, Jen. “Primary microRNA processing in humans: biology, biotechnology and disease.” 2017. Web. 05 Mar 2021.

Vancouver:

Quick-Cleveland J. Primary microRNA processing in humans: biology, biotechnology and disease. [Internet] [Thesis]. UCLA; 2017. [cited 2021 Mar 05]. Available from: http://www.escholarship.org/uc/item/4sh028f3.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Quick-Cleveland J. Primary microRNA processing in humans: biology, biotechnology and disease. [Thesis]. UCLA; 2017. Available from: http://www.escholarship.org/uc/item/4sh028f3

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

19. Shersher, Elena. The Influence of the Proximal Thiolate Ligand and Hydrogen Bond Network of the Proximal Helix on the Structural and Biochemical Properties of Chloroperoxidase.

Degree: PhD, Biochemistry, 2016, Florida International University

URL: https://digitalcommons.fiu.edu/etd/2483 ; 10.25148/etd.FIDC000241 ; FIDC000241

► Chloroperoxidase (CPO) from Caldariomyces fumago is a versatile heme enzyme with great potential for environmental and pharmaceutical applications. It catalyzes a plethora of reactions… (more)

▼ Chloroperoxidase (CPO) from Caldariomyces fumago is a versatile heme enzyme with great potential for environmental and pharmaceutical applications. It catalyzes a plethora of reactions including halogenation, dismutation, epoxidation, and oxidation. The diverse catalytic capabilities of CPO have long been attributed to the protein’s distinct active site that combines structural features of peroxidases and cytochromes P450. Particularly, the role of the axial thiolate ligand in CPO catalysis has been much debated. Furthermore, no data are available on the role of hydrogen bonding between Arg 26-Asn 37 and Ala 27-Asn 33 of the proximal helix in defining the structural and catalytic properties of CPO. In order to investigate the influence of the proximal thiolate and the proximal hydrogen bond network on the structural and biochemical properties of CPO, several mutant CPOs were constructed and characterized using various spectroscopic techniques and enzymatic assays. Cysteine 29, which coordinates to the heme, was replaced with a His (C29H) to mimic the proximal ligation of classical peroxidases. The UV-Vis spectrum of the carbon monoxide complex of ferrous C29H mutant remained essentially identical to that of wild type (WT) CPO and P450 although the ferric state of the variant enzyme showed a spectral pattern reminiscent of a classical histidine ligated heme peroxidase. Histidine ligation was further confirmed by paramagnetic NMR spectroscopy. Contrary to a previous report, the specific chlorination activity of C29H was essentially abolished (less than 1% of that of WT CPO) but the epoxidation and peroxidation activities were enhanced 10-fold and 55-fold, respectively. These findings demonstrate for the first time that the heme ligand, Cys 29 in CPO, is not a prerequisite for CPO’s unique P450-like spectroscopic signatures but is constitutive for the protein’s versatile catalytic activities. Arginine 26 and Asparagine 33 in the proximal heme pocket were replaced with Ala (R26A, N33A, and R26A/N33A) to disrupt hydrogen bonding. Tertiary structures and heme environments of R26A, N33A, and R26A/N33A differed from those of WT CPO as determined by CD spectroscopy. The specific chlorination and dismutation activities of all mutants were almost abolished but the peroxidation and epoxidation rates were increased. These results show that the proximal hydrogen bond network plays an important role in maintaining the structure and catalytic diversity of CPO. Advisors/Committee Members: Xiaotang Wang, Yuan Liu, David C. Chatfield, Watson J. Lees, Lou W. Kim.

Subjects/Keywords: Chloroperoxidase; Peroxygenase; Heme Protein; Catalysis; Proximal Thiolate; Hydrogen Bond Network; Biochemistry; Biotechnology

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APA (6^th Edition):

Shersher, E. (2016). The Influence of the Proximal Thiolate Ligand and Hydrogen Bond Network of the Proximal Helix on the Structural and Biochemical Properties of Chloroperoxidase. (Doctoral Dissertation). Florida International University. Retrieved from https://digitalcommons.fiu.edu/etd/2483 ; 10.25148/etd.FIDC000241 ; FIDC000241

Chicago Manual of Style (16^th Edition):

Shersher, Elena. “The Influence of the Proximal Thiolate Ligand and Hydrogen Bond Network of the Proximal Helix on the Structural and Biochemical Properties of Chloroperoxidase.” 2016. Doctoral Dissertation, Florida International University. Accessed March 05, 2021. https://digitalcommons.fiu.edu/etd/2483 ; 10.25148/etd.FIDC000241 ; FIDC000241.

MLA Handbook (7^th Edition):

Shersher, Elena. “The Influence of the Proximal Thiolate Ligand and Hydrogen Bond Network of the Proximal Helix on the Structural and Biochemical Properties of Chloroperoxidase.” 2016. Web. 05 Mar 2021.

Vancouver:

Shersher E. The Influence of the Proximal Thiolate Ligand and Hydrogen Bond Network of the Proximal Helix on the Structural and Biochemical Properties of Chloroperoxidase. [Internet] [Doctoral dissertation]. Florida International University; 2016. [cited 2021 Mar 05]. Available from: https://digitalcommons.fiu.edu/etd/2483 ; 10.25148/etd.FIDC000241 ; FIDC000241.

Council of Science Editors:

Shersher E. The Influence of the Proximal Thiolate Ligand and Hydrogen Bond Network of the Proximal Helix on the Structural and Biochemical Properties of Chloroperoxidase. [Doctoral Dissertation]. Florida International University; 2016. Available from: https://digitalcommons.fiu.edu/etd/2483 ; 10.25148/etd.FIDC000241 ; FIDC000241

Florida International University

20. Kwong Lam, Elwood. Investigating the Role of the Proximal Cysteine Hydrogen Bonding Network and Distal Pocket in Chloroperoxidase.

Degree: PhD, Biochemistry, 2018, Florida International University

URL: https://digitalcommons.fiu.edu/etd/3898 ; 10.25148/etd.FIDC007009 ; FIDC007009

► Chloroperoxidase (CPO) is one of the most versatile heme enzyme isolated from the marine fungus, Caldariomyces fumago. Functionally, CPO can catalyze four types of… (more)

▼ Chloroperoxidase (CPO) is one of the most versatile heme enzyme isolated from the marine fungus, Caldariomyces fumago. Functionally, CPO can catalyze four types of reactions: peroxidation (peroxidase-like), dismutation (catalase-like), halogenation (halogenase-like), and peroxygenation (P450-like). Structurally, CPO has a distal and proximal pockets that can be best described as a hybrid of classical peroxidase and P450s. As a heme-thiolate protein, CPO contains the conserved proximal Pro28-Cys29-Pro30 stretch found in other members of the family. However, the structural and functional roles of these proline residues remain poorly understood. Site-directed mutagenesis was undertaken to generates three CPO mutants, P28A-, P30A-, P28A/P30A-CPO. The replacement of the rigid proline with a more flexible alanine residue, freed up the back bone amide for the formation of additional amide-sulfur hydrogen bond, allowing the investigation of the importance of these residues in CPO catalysis. The three CPO mutants displayed dramatic difference in ligand binding affinity and catalytic activities relative to WT-CPO. Any mutations on the proline resides within the proximal loop eliminated the halogenation and dismutation activities but enhanced the vii epoxidation and peroxidation activities by 4-14 fold. As the binding affinity for cyanide, the CPO mutants displayed significantly higher dissociation constant relative to WT-CPO. Our results revealed that Pro28 and Pro30 play important roles in maintaining the versatility of CPO. As a versatile enzyme, CPO has great application potential in pharmaceutical and chemical industry due to its ability to catalyze the formation of chiral epoxides. Phe103 and Phe186 located on the distal pocket have been proposed to guard the access of substrates to the ferryl oxygen of the heme center. The interactions of these two phenylalanine residues restricted the size of substrates and regulates CPO’s enantioselectivity. F186A- and F103A/F186A-CPO were generated and characterized where the rate of peroxidation and epoxidation were significantly enhanced at the expense of halogenation and dismutation activities. Our results demonstrated that Phe186 played a subtler role relative to Phe103 in terms of substrate specificity and product enantioselectivity of CPO. Advisors/Committee Members: Xiaotang Wang, David Chatfield, Yuan Liu, Watson Lees, Alejandro Barbieri.

Subjects/Keywords: Chloroperoxidase; Peroxygenase; Heme Protein; Catalysis; Proximal Thiolate; Hydrogen Bond Network; Distal Pocket; Biochemistry

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Kwong Lam, E. (2018). Investigating the Role of the Proximal Cysteine Hydrogen Bonding Network and Distal Pocket in Chloroperoxidase. (Doctoral Dissertation). Florida International University. Retrieved from https://digitalcommons.fiu.edu/etd/3898 ; 10.25148/etd.FIDC007009 ; FIDC007009

Chicago Manual of Style (16^th Edition):

Kwong Lam, Elwood. “Investigating the Role of the Proximal Cysteine Hydrogen Bonding Network and Distal Pocket in Chloroperoxidase.” 2018. Doctoral Dissertation, Florida International University. Accessed March 05, 2021. https://digitalcommons.fiu.edu/etd/3898 ; 10.25148/etd.FIDC007009 ; FIDC007009.

MLA Handbook (7^th Edition):

Kwong Lam, Elwood. “Investigating the Role of the Proximal Cysteine Hydrogen Bonding Network and Distal Pocket in Chloroperoxidase.” 2018. Web. 05 Mar 2021.

Vancouver:

Kwong Lam E. Investigating the Role of the Proximal Cysteine Hydrogen Bonding Network and Distal Pocket in Chloroperoxidase. [Internet] [Doctoral dissertation]. Florida International University; 2018. [cited 2021 Mar 05]. Available from: https://digitalcommons.fiu.edu/etd/3898 ; 10.25148/etd.FIDC007009 ; FIDC007009.

Council of Science Editors:

Kwong Lam E. Investigating the Role of the Proximal Cysteine Hydrogen Bonding Network and Distal Pocket in Chloroperoxidase. [Doctoral Dissertation]. Florida International University; 2018. Available from: https://digitalcommons.fiu.edu/etd/3898 ; 10.25148/etd.FIDC007009 ; FIDC007009

University of Montana

21. Nold, Shiloh M. EVOLUTION OF THE KINETICS AND DYNAMICS OF HEME-CREVICE LOOP REGULATING CHEMISTRY IN HUMAN CYTOCHROME C.

Degree: MS, 2017, University of Montana

URL: https://scholarworks.umt.edu/etd/10945

► Cytochrome c, cytc, is a metalloprotein that plays primary roles in electron transport and intrinsic apoptotic pathways. Much of the chemistry that cytc is… (more)

▼ Cytochrome c, cytc, is a metalloprotein that plays primary roles in electron transport and intrinsic apoptotic pathways. Much of the chemistry that cytc is involved with is regulated by a highly conserved region known as the heme crevice loop, consisting of residues 70-85. Only three of these residues (those at positions 81, 83 and 85) are not universally conserved within the evolutionary timeline. Here I look to elucidate possible evolutionary roles for several of the key residues known to be important in regulating heme chemistry of cytc. I first address the role that lysine 72 plays in cytc folding and chemistry. Here I provide evidence that K72 alters the alkaline conformational transition of cytc. Trimethylated lysine 72, tmK72, was previously investigated and shows similar trends in peroxidase activity (McClelland et al 2013). Lastly I address I81 which is not only within the heme crevice loop and not universally conserved, but is also a hydrophobic surface residue. Here I make a Hu I81A variant, mutating to the alanine seen in yeast cytc. Our hypothesis was that this mutation would show a destabilization of the heme crevice loop region when monitoring the charge transfer band (695 nm), and more importantly observing an increase in peroxidase activity when monitoring for tetraguaiacol (470 nm) in our enzymatic assay. This signifies this mutation could have evolved to lock down that heme crevice loop in order to decrease peroxidase activity when intrinsic apoptosis pathways evolved in mammals. pH titration data showed a decrease in stability of the alkaline conformational transition in our I81A variant when compared to Hu WT. When looking at peroxidase activity we see a significant increase in k_cat(s^-1) values of I81A compared to Hu WT. The Hu I81A indeed shows what we would expect of a mutation which evolved to decrease peroxidase activity. Analysis of pH jump data in the Soret region of cytc shows that there is an effect on lysine 73 or 79 bound alkaline ligands (unable to be determined) by a decrease in amplitude, however there is no effect on the lysine 72 bound alkaline ligand.

Subjects/Keywords: Cytochrome c; K72A; I81A; Heme Crevice Loop; alkaline conformational transition; proline isomerization; Biochemistry; Biophysics

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APA (6^th Edition):

Nold, S. M. (2017). EVOLUTION OF THE KINETICS AND DYNAMICS OF HEME-CREVICE LOOP REGULATING CHEMISTRY IN HUMAN CYTOCHROME C. (Masters Thesis). University of Montana. Retrieved from https://scholarworks.umt.edu/etd/10945

Chicago Manual of Style (16^th Edition):

Nold, Shiloh M. “EVOLUTION OF THE KINETICS AND DYNAMICS OF HEME-CREVICE LOOP REGULATING CHEMISTRY IN HUMAN CYTOCHROME C.” 2017. Masters Thesis, University of Montana. Accessed March 05, 2021. https://scholarworks.umt.edu/etd/10945.

MLA Handbook (7^th Edition):

Nold, Shiloh M. “EVOLUTION OF THE KINETICS AND DYNAMICS OF HEME-CREVICE LOOP REGULATING CHEMISTRY IN HUMAN CYTOCHROME C.” 2017. Web. 05 Mar 2021.

Vancouver:

Nold SM. EVOLUTION OF THE KINETICS AND DYNAMICS OF HEME-CREVICE LOOP REGULATING CHEMISTRY IN HUMAN CYTOCHROME C. [Internet] [Masters thesis]. University of Montana; 2017. [cited 2021 Mar 05]. Available from: https://scholarworks.umt.edu/etd/10945.

Council of Science Editors:

Nold SM. EVOLUTION OF THE KINETICS AND DYNAMICS OF HEME-CREVICE LOOP REGULATING CHEMISTRY IN HUMAN CYTOCHROME C. [Masters Thesis]. University of Montana; 2017. Available from: https://scholarworks.umt.edu/etd/10945

University of California – Berkeley

22. Winter, Michael B. Tuning Sensing and Signaling in the H-NOX Family of Heme Proteins.

Degree: Chemistry, 2011, University of California – Berkeley

URL: http://www.escholarship.org/uc/item/8t90r4s2

► Nitric oxide (NO) signaling in mammals occurs through activation of the soluble isoform of guanylate cyclase (sGC), which results in diverse physiological processes such as… (more)

▼ Nitric oxide (NO) signaling in mammals occurs through activation of the soluble isoform of guanylate cyclase (sGC), which results in diverse physiological processes such as blood vessel dilation and neurotransmission. sGC is a heterodimeric heme protein that has evolved to be a specific sensor for NO. Although sGC contains the same histidyl-ligated porphyrin as the globins, it has no measureable affinity for oxygen and does not oxidize in air. These unusual features facilitate selective and robust activation by NO in aerobic cellular contexts. Questions regarding the mechanism of ligand discrimination in sGC led to the identification of sGC heme domain homologues in many different organisms where these proteins function as NO and/or oxygen sensors for gas-mediated signaling pathways. The members of the protein family have been subsequently termed Heme Nitric oxide/OXygen binding (H-NOX) domains due to their divergent ligand-binding properties. Functional characterization of H-NOX domains from prokaryotes has provided important clues about the structural features that control ligand discrimination across the H-NOX family. However, additional fundamental questions remain about the influence of protein structure on heme chemistry. Extensive studies on the globins, as model heme proteins, have established the functional importance of heme protein topological features in modulating gas diffusion to and from the heme site. In globins, deep gas pockets around the porphyrin transiently capture and release oxygen, tuning oxygen affinity for transport, delivery, and storage in diverse physiological environments. Although mechanisms of gas binding in H-NOX proteins have been a subject of intense investigation, there is little knowledge regarding the functional role of protein structure in modulating gas diffusion. Using X-ray crystallography with xenon and kinetic measurements, a tunnel network that extends between the solvent and interior heme site was mapped in a prokaryotic H-NOX domain. Hindering gas diffusion through the tunnels has important consequences on diatomic gas affinity. This suggests that protein tunnels in H-NOX proteins may play functional roles in tuning gas-mediated signaling. Unlike isolated H-NOX domains, mammalian sGC is a structurally more complex, multi-domain protein. The ability of the sGC heme to resist oxidation in air is unique among histidyl-ligated heme proteins and essential for maximal NO-induced activation. Speculations have been made about how the sGC heme resists oxidation, but no study has systemically addressed the structural and electronic factors that contribute to this critical property. To probe the accessibility of oxygen to the heme site, we sought to substitute the native heme of sGC with an unnatural porphyrin displaying emission that is quenched by oxygen. Using an expression-based methodology, a phosphorescent Ru porphyrin was incorporated in sGC constructs of varying lengths. Emission quenching results suggest that oxygen diffusion to the full-length sGC heme site is…

Subjects/Keywords: Chemistry; Biochemistry; Molecular biology; Diatomic gas signaling; Heme; Hemoprotein; H-NOX; Sensing; Soluble Guanylate Cyclase (sGC)

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APA (6^th Edition):

Winter, M. B. (2011). Tuning Sensing and Signaling in the H-NOX Family of Heme Proteins. (Thesis). University of California – Berkeley. Retrieved from http://www.escholarship.org/uc/item/8t90r4s2

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Winter, Michael B. “Tuning Sensing and Signaling in the H-NOX Family of Heme Proteins.” 2011. Thesis, University of California – Berkeley. Accessed March 05, 2021. http://www.escholarship.org/uc/item/8t90r4s2.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Winter, Michael B. “Tuning Sensing and Signaling in the H-NOX Family of Heme Proteins.” 2011. Web. 05 Mar 2021.

Vancouver:

Winter MB. Tuning Sensing and Signaling in the H-NOX Family of Heme Proteins. [Internet] [Thesis]. University of California – Berkeley; 2011. [cited 2021 Mar 05]. Available from: http://www.escholarship.org/uc/item/8t90r4s2.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Winter MB. Tuning Sensing and Signaling in the H-NOX Family of Heme Proteins. [Thesis]. University of California – Berkeley; 2011. Available from: http://www.escholarship.org/uc/item/8t90r4s2

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of California – Irvine

23. Hollingsworth, Scott Alan. At the interface of experiment and computation: explorations of heme protein redox partner interactions, water behavior on organic surfaces and other systems.

Degree: Biological Sciences, 2016, University of California – Irvine

URL: http://www.escholarship.org/uc/item/9fj2b88j

► In part one of this thesis, the interactions and resulting complexes between heme proteins and their associated electron-transferring redox partner proteins, termed here as heme… (more)

▼ In part one of this thesis, the interactions and resulting complexes between heme proteins and their associated electron-transferring redox partner proteins, termed here as heme protein redox partners, are carefully studied. Such complexes navigate a delicate balance between achieving fast turnover and tight, specific binding. To probe how Nature has balanced these seemingly opposing forces, a series of studies were conducted on three separate heme protein redox partner systems that have achieved a working balance using different approaches; Cytochrome P450cam and its redox partner putidaredoxin, Leishmania major peroxidase and its partner Leishmania major cytochrome c and finally the multi-domain nitric oxide synthase. Each system was initially probed using computational methods including molecular dynamics, Brownian dynamics, and modeling before being experimentally validated against previous findings, novel studies or both. In part two, the focus is shifted from protein interactions to water behavior on organic surfaces. Studying the behavior of water on such organic surfaces can have wide-ranging impacts on our understanding of not only fundamental water dynamics, but also atmospheric chemistry and chemistry on urban surfaces. Self-assembled monolayers (or SAMs) have long served as a model system to probe how differences in organic surface chemistry may affect water behavior. To this point, the behavior of water on a variety of SAMs were investigated using molecular dynamics in a series of studies including one with experimental validation to deepen our understanding of the dependence of water behavior on the structural makeup of both a pristine idealized surface and more realistic defective SAM systems.Finally, three additional separate studies are presented in the third and last part of this thesis. These distinct and independent studies 1) cover the conformational dependence of a central protein residue on the conformation of its neighbors, 2) computationally study the binding of a membrane associated protein to a target lipid in a lipid bilayer and 3) experimentally determine the crystal structure of Bacilus subtillis arginase. When combined with the two series of studies previously presented in this thesis, the great potential in applying a combined experimental and computational approach to address unanswered questions is highlighted and explored.

Subjects/Keywords: Biochemistry; Biophysics; Physical chemistry; computational biology; heme protein; molecular dynamics; protein conformation; protein redox partner; self-assembled monolayer

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APA (6^th Edition):

Hollingsworth, S. A. (2016). At the interface of experiment and computation: explorations of heme protein redox partner interactions, water behavior on organic surfaces and other systems. (Thesis). University of California – Irvine. Retrieved from http://www.escholarship.org/uc/item/9fj2b88j

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Hollingsworth, Scott Alan. “At the interface of experiment and computation: explorations of heme protein redox partner interactions, water behavior on organic surfaces and other systems.” 2016. Thesis, University of California – Irvine. Accessed March 05, 2021. http://www.escholarship.org/uc/item/9fj2b88j.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Hollingsworth, Scott Alan. “At the interface of experiment and computation: explorations of heme protein redox partner interactions, water behavior on organic surfaces and other systems.” 2016. Web. 05 Mar 2021.

Vancouver:

Hollingsworth SA. At the interface of experiment and computation: explorations of heme protein redox partner interactions, water behavior on organic surfaces and other systems. [Internet] [Thesis]. University of California – Irvine; 2016. [cited 2021 Mar 05]. Available from: http://www.escholarship.org/uc/item/9fj2b88j.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Hollingsworth SA. At the interface of experiment and computation: explorations of heme protein redox partner interactions, water behavior on organic surfaces and other systems. [Thesis]. University of California – Irvine; 2016. Available from: http://www.escholarship.org/uc/item/9fj2b88j

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of California – Berkeley

24. Tran, Rosalie. Probing the heme structure and environment of bacterial Heme-Nitric oxide/OXygen binding domains with resonance Raman spectroscopy.

Degree: Chemistry, 2010, University of California – Berkeley

URL: http://www.escholarship.org/uc/item/6dh6g97q

► The Heme-Nitric oxide/OXygen binding (H-NOX) domain encompasses a family of proteins closely related (≤ 40% sequence identity) to the heme domain of soluble guanylate cyclase… (more)

▼ The Heme-Nitric oxide/OXygen binding (H-NOX) domain encompasses a family of proteins closely related (≤ 40% sequence identity) to the heme domain of soluble guanylate cyclase (sGC), the eukaryotic enzyme receptor for NO [1, 2]. sGC discriminates between NO and O₂, and exclusively binds NO even in the presence of excess O₂. Although some H-NOX domains have ligand binding properties that are identical to sGC, others additionally bind O₂, including the atypical sGCs from Drosophila melanogaster and Caenorhabditis elegans [1, 3, 4]. The molecular basis of this ligand selectivity is not fully understood. In order to better understand the H-NOX domain, resonance Raman (RR) spectroscopy was employed in combination with isotopic substitution and site-directed mutagenesis to probe the heme pocket in Thermoanaerobacter tengcongensis (Tt H-NOX) as a model system for this family of heme proteins. Thus, the expression, purification, and RR characterization of Tt H-NOX and selected mutants were performed to elucidate the heme environmental properties that influence ligand binding.A striking feature of the O₂-bound WT Tt H-NOX crystal structure is the presence of a distorted heme molecule [5]. RR investigation of Tt H-NOX proteins containing mutations at key conserved residues, Ile-5 and Pro-115, determined that the most dramatic heme conformational changes occurred in the O₂-bound forms, and that the single P115A mutation generated a significantly relaxed chromophore. Decreased RR intensities were observed for several out-of-plane modes in the 400-750 cm^-1 region known to be sensitive to ruffling and saddling deformations, as well as increased vibrational frequencies for the core heme skeletal modes. These changes demonstrated that the P115A heme conformation was considerably more relaxed than WT, with increased flexibility within the protein pocket that allowed for rapid sampling of alternate conformations.Another remarkable feature of this family is the spectroscopic observation of an unusually high ν(C-O) frequency. To elucidate the interactions responsible for this property, mutations were made in Tt H-NOX to probe the distal pocket, the conserved Tyr-Ser-Arg (YxSxR) motif, and the heme-linkage site (His-102). RR spectra of these mutants indicated that H-bonding interactions between these residues and the heme significantly affected the CO bond by increasing the back-donation of the Fe^II d<sub>π</sub> electrons into the CO π^* orbitals. The most significant change occurred upon disruption of the H-bonds between the YxSxR motif and the heme propionate groups, producing two dominant CO-bound heme conformations; one was structurally similar to WT, and the other conformer displayed ν(C-O) downshifts of up to ~70…

Subjects/Keywords: Chemistry, Biochemistry; Biophysics, General; H-NOX; heme proteins; ligand binding; resonance Raman spectroscopy; soluble guanylate cyclase; Thermoanaerobacter tengcongensis

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APA (6^th Edition):

Tran, R. (2010). Probing the heme structure and environment of bacterial Heme-Nitric oxide/OXygen binding domains with resonance Raman spectroscopy. (Thesis). University of California – Berkeley. Retrieved from http://www.escholarship.org/uc/item/6dh6g97q

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Tran, Rosalie. “Probing the heme structure and environment of bacterial Heme-Nitric oxide/OXygen binding domains with resonance Raman spectroscopy.” 2010. Thesis, University of California – Berkeley. Accessed March 05, 2021. http://www.escholarship.org/uc/item/6dh6g97q.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Tran, Rosalie. “Probing the heme structure and environment of bacterial Heme-Nitric oxide/OXygen binding domains with resonance Raman spectroscopy.” 2010. Web. 05 Mar 2021.

Vancouver:

Tran R. Probing the heme structure and environment of bacterial Heme-Nitric oxide/OXygen binding domains with resonance Raman spectroscopy. [Internet] [Thesis]. University of California – Berkeley; 2010. [cited 2021 Mar 05]. Available from: http://www.escholarship.org/uc/item/6dh6g97q.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Tran R. Probing the heme structure and environment of bacterial Heme-Nitric oxide/OXygen binding domains with resonance Raman spectroscopy. [Thesis]. University of California – Berkeley; 2010. Available from: http://www.escholarship.org/uc/item/6dh6g97q

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

25. Matz, Kayla Louise Polzin. The Intricate Balance of Metal Trafficking in Bacteria: Import of Iron in Bacillus anthracis and Export of Excess Copper in Escherichia coli .

Degree: 2015, University of Arizona

URL: http://hdl.handle.net/10150/581322

► Bacterial organisms continuously maintain homeostasis even in changing environments. This ability to maintain homeostasis is especially critical for pathogenic and opportunistic bacteria, which must adapt… (more)

▼ Bacterial organisms continuously maintain homeostasis even in changing environments. This ability to maintain homeostasis is especially critical for pathogenic and opportunistic bacteria, which must adapt to both abiotic and biotic host environments. Both types of environments present unique limitations and conditions. Transition metal homeostasis under these varying conditions is important for bacterial survival. Transition metals such as zinc, cobalt, iron and copper are essential for cell survival, but become toxic if in excess. The host organism often takes advantage of this requirement by greatly limiting access to transition metals to limit infections, but in other environments, toxic levels of metal may be present. Bacterial organisms have developed many mechanisms to maintain transition metal homeostasis. This study focuses on two bacterial systems that are utilized to maintain metal balance; the heme-acquiring iron surface determinant (Isd) system of Bacillus anthracis and the copper and silver export Cus system of Escherichia coli. Host organisms use many proteins and systems to limit iron access from pathogenic bacteria, known as nutrient immunity. B. anthracis must acquire iron from the host organism upon infection and so has evolved multiple iron acquisition systems. The Isd system employs two extracellular proteins, IsdX1 and IsdX2, to remove heme from hemoglobin to use as an iron source. Once bound to heme, these hemophores transfer heme to a cell surface attached protein, IsdC, which further relays the molecule to be transferred into the cell for iron use. This study focused on the kinetics of heme transfer to better understand how acquisition occurs. This study determined that the oxidation state of the iron-heme molecule plays a significant role in the kinetics of heme acquisition by IsdX1 and subsequent transfer to IsdC. This work clarifies and further establishes the mechanism of iron acquisition by B. anthracis during infection. Copper and silver are used in many settings as antimicrobial agents, including as an alternative to antibiotic drugs. Pathogenic and opportunistic bacteria, such as E. coli, experience stress upon contact with copper and silver surfaces and materials. Copper is an essential transition metal, while silver is not biologically used, but both become toxic when in excess due to redox properties and disruption of biological molecules. E. coli utilizes several systems to remove excess copper and silver to resist toxicity. The Cus system, consisting of the soluble CusF and tripartite pump CusCBA, specifically exports copper and silver from the periplasm. Several roles of CusF have been suggested from in vitro data. The components CusAB were hypothesized to be the essential proteins of the CusCBA pump, while the outer membrane unit may not contribute specificity or be necessary for export. This study focused on the role and importance of CusF and outer membrane channel CusC during copper stress in vivo. An in vivo interaction between CusF and CusB was identified during copper… Advisors/Committee Members: McEvoy, Megan (advisor), McEvoy, Megan (committeemember), Ghosh, Indraneel (committeemember), Horton, Nancy (committeemember), Tomat, Elisa (committeemember).

Subjects/Keywords: Cus; heme acquisition; Isd; Biochemistry; copper resistance

…of heme/hemin-protein complexes under Table 2.2 83 reduced and oxidized conditions Table… …2.3 Rates of Fe3+-hemin transfer 87 Table 2.4 Rates of Fe2+-heme transfer 88 Table 3.1… …affinity for ferric hemin than ferrous heme, and as mentioned above, upon oxidation tetramer… …71 2.3.3 Heme extraction… …73 2.3.4 Heme loading…

12 more images…

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Matz, K. L. P. (2015). The Intricate Balance of Metal Trafficking in Bacteria: Import of Iron in Bacillus anthracis and Export of Excess Copper in Escherichia coli . (Doctoral Dissertation). University of Arizona. Retrieved from http://hdl.handle.net/10150/581322

Chicago Manual of Style (16^th Edition):

Matz, Kayla Louise Polzin. “The Intricate Balance of Metal Trafficking in Bacteria: Import of Iron in Bacillus anthracis and Export of Excess Copper in Escherichia coli .” 2015. Doctoral Dissertation, University of Arizona. Accessed March 05, 2021. http://hdl.handle.net/10150/581322.

MLA Handbook (7^th Edition):

Matz, Kayla Louise Polzin. “The Intricate Balance of Metal Trafficking in Bacteria: Import of Iron in Bacillus anthracis and Export of Excess Copper in Escherichia coli .” 2015. Web. 05 Mar 2021.

Vancouver:

Matz KLP. The Intricate Balance of Metal Trafficking in Bacteria: Import of Iron in Bacillus anthracis and Export of Excess Copper in Escherichia coli . [Internet] [Doctoral dissertation]. University of Arizona; 2015. [cited 2021 Mar 05]. Available from: http://hdl.handle.net/10150/581322.

Council of Science Editors:

Matz KLP. The Intricate Balance of Metal Trafficking in Bacteria: Import of Iron in Bacillus anthracis and Export of Excess Copper in Escherichia coli . [Doctoral Dissertation]. University of Arizona; 2015. Available from: http://hdl.handle.net/10150/581322

Indian Institute of Science

26. Narayan, Karthik K. Electrochemical Detection Of Proteins : Myoglobin As A Case Study.

Degree: MS, Faculty of Science, 2015, Indian Institute of Science

URL: http://etd.iisc.ac.in/handle/2005/2482

► An effective electrochemical sensor for myoglobin (Myb) detection was developed using a simple procedure of denaturing the protein with guanidine hydrochloride and detecting the released… (more)

Subjects/Keywords: Electrochemical Sensors; Proteins - Electrochemical Detection; Myoglobins - Electrochemical Detection; Myoglobin; Proteins as Biomarkers; Titania Nanotubes (TNT); Heme Proteins; Myb; Biochemistry

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APA (6^th Edition):

Narayan, K. K. (2015). Electrochemical Detection Of Proteins : Myoglobin As A Case Study. (Masters Thesis). Indian Institute of Science. Retrieved from http://etd.iisc.ac.in/handle/2005/2482

Chicago Manual of Style (16^th Edition):

Narayan, Karthik K. “Electrochemical Detection Of Proteins : Myoglobin As A Case Study.” 2015. Masters Thesis, Indian Institute of Science. Accessed March 05, 2021. http://etd.iisc.ac.in/handle/2005/2482.

MLA Handbook (7^th Edition):

Narayan, Karthik K. “Electrochemical Detection Of Proteins : Myoglobin As A Case Study.” 2015. Web. 05 Mar 2021.

Vancouver:

Narayan KK. Electrochemical Detection Of Proteins : Myoglobin As A Case Study. [Internet] [Masters thesis]. Indian Institute of Science; 2015. [cited 2021 Mar 05]. Available from: http://etd.iisc.ac.in/handle/2005/2482.

Council of Science Editors:

Narayan KK. Electrochemical Detection Of Proteins : Myoglobin As A Case Study. [Masters Thesis]. Indian Institute of Science; 2015. Available from: http://etd.iisc.ac.in/handle/2005/2482

Western Washington University

27. Hall, James M. (James Morgan). ¹⁵N Heteronuclear Single Quantum Coherence backbone assignment of cyanomet isoform sperm whale myoglobin and permutant.

Degree: MS, Chemistry, 2013, Western Washington University

URL: https://doi.org/10.25710/zx05-bd88 ; https://cedar.wwu.edu/wwuet/296

► The relationship between backbone dynamics and stability in circularly permuted globins is not well understood. HGL16 is a circular permutant of sperm whale myoglobin… (more)

▼ The relationship between backbone dynamics and stability in circularly permuted globins is not well understood. HGL16 is a circular permutant of sperm whale myoglobin (sw Mb) in which the amino and carboxyl termini have been linked by 16 amino acids, (GlyGlyGlySer)4. New termini have been generated between the G and H helices. This permutant was shown to be 5.2 kcal/mol less stable than the wild-type protein. Backbone dynamic studies of permuted globins via 15N Heteronuclear Single Quantum Coherence (NHSQC) nuclear magnetic resonance (NMR) experiments may help achieve a better understanding to the observed stability changes observed. The assignments of both wild-type sw Mb and HGL16 NHSQC spectra are necessary to perform backbone dynamics studies. HGL16 has been previously produced in E. coli cells, but with low soluble expression yields. Generating 15N HSQC spectra and assigning the backbone amide resonances for dynamic studies requires 15N/13C isotopic labeling. Isotopic labeling requires expression of myoglobins in a minimal medium, which typically gives significantly lower yields compared to protein expression rich medium. An alternate approach is expression of the labeled proteins in the apo-form as inclusion bodies, followed by reconstitution of the holo-form with the heme prosthetic group. Purification and reconstitution of the globins from inclusion bodies, gave higher yields compared to soluble expression in minimal medium. Mass spectrometry was used to verify the identities of the purified globins. Reconstituted proteins were characterized by UV-Vis spectroscopy, and one dimensional proton NMR. These findings show the heme binding in the reconstituted globin is very similar to that in the holoprotein purified from the soluble fraction. 15N /13C isotopic labeling in minimal medium was successful. Two dimensional NHSQC spectra for the cyanomet isoform of wild-type sw Mb and HGL16 were acquired, and the peaks were assigned using data from the following three dimensional experiments: HNCA, HN(CO)CA, HNCACB, CBCA(CO)NH. The assignment of the NHSQC spectrum of HGL16 permutein required additional data from HNCO and HN(CA)CO experiments. Advisors/Committee Members: Anthony-Cahill, Spencer J., Smirnov, Sergey L., Spiegel, P. Clint.

Subjects/Keywords: Chemistry; Myoglobin; Sperm whale – Physiology; Proteins – Chemical modification; Heme – Synthesis; Nuclear magnetic resonance spectroscopy; Ligand binding (Biochemistry); masters theses

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APA (6^th Edition):

Hall, J. M. (. M. (2013). ¹⁵N Heteronuclear Single Quantum Coherence backbone assignment of cyanomet isoform sperm whale myoglobin and permutant. (Masters Thesis). Western Washington University. Retrieved from https://doi.org/10.25710/zx05-bd88 ; https://cedar.wwu.edu/wwuet/296

Chicago Manual of Style (16^th Edition):

Hall, James M (James Morgan). “¹⁵N Heteronuclear Single Quantum Coherence backbone assignment of cyanomet isoform sperm whale myoglobin and permutant.” 2013. Masters Thesis, Western Washington University. Accessed March 05, 2021. https://doi.org/10.25710/zx05-bd88 ; https://cedar.wwu.edu/wwuet/296.

MLA Handbook (7^th Edition):

Hall, James M (James Morgan). “¹⁵N Heteronuclear Single Quantum Coherence backbone assignment of cyanomet isoform sperm whale myoglobin and permutant.” 2013. Web. 05 Mar 2021.

Vancouver:

Hall JM(M. ¹⁵N Heteronuclear Single Quantum Coherence backbone assignment of cyanomet isoform sperm whale myoglobin and permutant. [Internet] [Masters thesis]. Western Washington University; 2013. [cited 2021 Mar 05]. Available from: https://doi.org/10.25710/zx05-bd88 ; https://cedar.wwu.edu/wwuet/296.

Council of Science Editors:

Hall JM(M. ¹⁵N Heteronuclear Single Quantum Coherence backbone assignment of cyanomet isoform sperm whale myoglobin and permutant. [Masters Thesis]. Western Washington University; 2013. Available from: https://doi.org/10.25710/zx05-bd88 ; https://cedar.wwu.edu/wwuet/296

Virginia Commonwealth University

28. Belvin, Benjamin. HcpR of Porphyromonas gingivalis utilizes heme to bind NO.

Degree: MS, Biochemistry, 2014, Virginia Commonwealth University

URL: https://doi.org/10.25772/C4Y2-PJ04 ; https://scholarscompass.vcu.edu/etd/639

► The obligate anaerobe Porphyromonas gingivalis is the etiological agent responsible for periodontal disease. It must withstand high levels of reactive nitrogen species in the oral… (more)

Subjects/Keywords: Porphyromonas gingivalis; Nitric oxide; NO; heme protein; nitrosative stress; nitrosative stress response; Biochemistry, Biophysics, and Structural Biology; Life Sciences

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APA (6^th Edition):

Belvin, B. (2014). HcpR of Porphyromonas gingivalis utilizes heme to bind NO. (Thesis). Virginia Commonwealth University. Retrieved from https://doi.org/10.25772/C4Y2-PJ04 ; https://scholarscompass.vcu.edu/etd/639

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Belvin, Benjamin. “HcpR of Porphyromonas gingivalis utilizes heme to bind NO.” 2014. Thesis, Virginia Commonwealth University. Accessed March 05, 2021. https://doi.org/10.25772/C4Y2-PJ04 ; https://scholarscompass.vcu.edu/etd/639.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Belvin, Benjamin. “HcpR of Porphyromonas gingivalis utilizes heme to bind NO.” 2014. Web. 05 Mar 2021.

Vancouver:

Belvin B. HcpR of Porphyromonas gingivalis utilizes heme to bind NO. [Internet] [Thesis]. Virginia Commonwealth University; 2014. [cited 2021 Mar 05]. Available from: https://doi.org/10.25772/C4Y2-PJ04 ; https://scholarscompass.vcu.edu/etd/639.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Belvin B. HcpR of Porphyromonas gingivalis utilizes heme to bind NO. [Thesis]. Virginia Commonwealth University; 2014. Available from: https://doi.org/10.25772/C4Y2-PJ04 ; https://scholarscompass.vcu.edu/etd/639

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Michigan State University

29. Yeh, Chen-Yu. New approaches to highly sterically encumbered porphyrins as heme active sites.

Degree: PhD, Department of Chemistry, 1999, Michigan State University

URL: http://etd.lib.msu.edu/islandora/object/etd:32591

Subjects/Keywords: Porphyrins – Synthesis; Binding sites (Biochemistry); Heme – Synthesis

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APA (6^th Edition):

Yeh, C. (1999). New approaches to highly sterically encumbered porphyrins as heme active sites. (Doctoral Dissertation). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:32591

Chicago Manual of Style (16^th Edition):

Yeh, Chen-Yu. “New approaches to highly sterically encumbered porphyrins as heme active sites.” 1999. Doctoral Dissertation, Michigan State University. Accessed March 05, 2021. http://etd.lib.msu.edu/islandora/object/etd:32591.

MLA Handbook (7^th Edition):

Yeh, Chen-Yu. “New approaches to highly sterically encumbered porphyrins as heme active sites.” 1999. Web. 05 Mar 2021.

Vancouver:

Yeh C. New approaches to highly sterically encumbered porphyrins as heme active sites. [Internet] [Doctoral dissertation]. Michigan State University; 1999. [cited 2021 Mar 05]. Available from: http://etd.lib.msu.edu/islandora/object/etd:32591.

Council of Science Editors:

Yeh C. New approaches to highly sterically encumbered porphyrins as heme active sites. [Doctoral Dissertation]. Michigan State University; 1999. Available from: http://etd.lib.msu.edu/islandora/object/etd:32591

Brock University

30. Maj, Mary C. A comparative study of protoheme and heme d catalases : role of the heme and the heme pocket in catalysis and ligand binding .

Degree: Department of Biological Sciences, 1996, Brock University

URL: http://hdl.handle.net/10464/1699

► Catalase dismutes H20 2 to O2 and H20. In successive twoelectron reactions H20 2 induces both oxidation and reduction at the heme group. In the… (more)

Subjects/Keywords: Heme oxygenase.; Catalase.; Ligand binding (Biochemistry); Catalysis.

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APA (6^th Edition):

Maj, M. C. (1996). A comparative study of protoheme and heme d catalases : role of the heme and the heme pocket in catalysis and ligand binding . (Thesis). Brock University. Retrieved from http://hdl.handle.net/10464/1699

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Maj, Mary C. “A comparative study of protoheme and heme d catalases : role of the heme and the heme pocket in catalysis and ligand binding .” 1996. Thesis, Brock University. Accessed March 05, 2021. http://hdl.handle.net/10464/1699.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Maj, Mary C. “A comparative study of protoheme and heme d catalases : role of the heme and the heme pocket in catalysis and ligand binding .” 1996. Web. 05 Mar 2021.

Vancouver:

Maj MC. A comparative study of protoheme and heme d catalases : role of the heme and the heme pocket in catalysis and ligand binding . [Internet] [Thesis]. Brock University; 1996. [cited 2021 Mar 05]. Available from: http://hdl.handle.net/10464/1699.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Maj MC. A comparative study of protoheme and heme d catalases : role of the heme and the heme pocket in catalysis and ligand binding . [Thesis]. Brock University; 1996. Available from: http://hdl.handle.net/10464/1699

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

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