+publisher:"University of Oklahoma" +contributor:("Richter-Addo, George B.")

University of Oklahoma

1. Warhausen, Adam Jared. SYNTHESIS, CHARACTERIZATION, ELECTROCHEMISTRY, AND SPECTROELECTROCHEMISTRY OF GROUP 8 METALLOPORPHYRIN COMPLEXES.

Degree: PhD, 2012, University of Oklahoma

URL: http://hdl.handle.net/11244/318994

► Chapter 4 describes the synthesis and characterization of 5-coordinate iron porphyrin complexes, where the 5th coordination site is occupied by a hydroxamate, acetate, or aryloxide… (more)

Subjects/Keywords: Porphyrins; Nitric oxide; Nitrosoamines; Hemoproteins

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APA (6^th Edition):

Warhausen, A. J. (2012). SYNTHESIS, CHARACTERIZATION, ELECTROCHEMISTRY, AND SPECTROELECTROCHEMISTRY OF GROUP 8 METALLOPORPHYRIN COMPLEXES. (Doctoral Dissertation). University of Oklahoma. Retrieved from http://hdl.handle.net/11244/318994

Chicago Manual of Style (16^th Edition):

Warhausen, Adam Jared. “SYNTHESIS, CHARACTERIZATION, ELECTROCHEMISTRY, AND SPECTROELECTROCHEMISTRY OF GROUP 8 METALLOPORPHYRIN COMPLEXES.” 2012. Doctoral Dissertation, University of Oklahoma. Accessed February 28, 2021. http://hdl.handle.net/11244/318994.

MLA Handbook (7^th Edition):

Warhausen, Adam Jared. “SYNTHESIS, CHARACTERIZATION, ELECTROCHEMISTRY, AND SPECTROELECTROCHEMISTRY OF GROUP 8 METALLOPORPHYRIN COMPLEXES.” 2012. Web. 28 Feb 2021.

Vancouver:

Warhausen AJ. SYNTHESIS, CHARACTERIZATION, ELECTROCHEMISTRY, AND SPECTROELECTROCHEMISTRY OF GROUP 8 METALLOPORPHYRIN COMPLEXES. [Internet] [Doctoral dissertation]. University of Oklahoma; 2012. [cited 2021 Feb 28]. Available from: http://hdl.handle.net/11244/318994.

Council of Science Editors:

Warhausen AJ. SYNTHESIS, CHARACTERIZATION, ELECTROCHEMISTRY, AND SPECTROELECTROCHEMISTRY OF GROUP 8 METALLOPORPHYRIN COMPLEXES. [Doctoral Dissertation]. University of Oklahoma; 2012. Available from: http://hdl.handle.net/11244/318994

University of Oklahoma

2. Powell, Samantha M. THE STRUCTURAL CHARACTERIZATION OF THE INTERACTIONS OF MYOGLOBIN, HEMOGLOBIN, C. DIFFICILE NITROREDUCTASE AND CYTOCHROME P450 WITH N-CONTAINING COMPOUNDS.

Degree: PhD, 2019, University of Oklahoma

URL: http://hdl.handle.net/11244/319369

► The overall goal of my work was to probe the structural biology of drug metabolite protein interactions and to correlate this with the negative side… (more)

▼ The overall goal of my work was to probe the structural biology of drug metabolite protein interactions and to correlate this with the negative side effects associated with many prescription drugs. More specifically, the focus was on the interactions of myoglobin (Mb), hemoglobin (Hb), a Clostridioides difficile nitroreductase (NR), and cytochrome P450 BM3-HD with N-containing compounds. Using a combination of spectroscopy and X-ray crystallography, I was able to accomplish this goal. In Chapter 2, the focus was on the formation of heme-nitroso adducts of Mb and Hb generated through oxidative and reductive pathways. While I initially predicted that heme-nitroso adducts would result from the reaction of Mb and Hb with nitro- and hydroxylamine-containing compounds, what actually resulted was the determination of a variety of products in addition to the predicted N-bound nitroso adducts. X-ray crystal structures of these products revealed that some of the compounds evaluated can indeed damage Hb through the formation of hemichromes that can be correlated with early stages of heme loss, which, downstream, may cause anemia. Additionally, we observed, for the first time, that two of the compounds evaluated are capable of S-nitrosating Hb at the betaCys93 residue, an important contributor to the transportation of NO throughout the body. And finally, one of the X-ray crystal structures displays a ligand trapped in a Xe pocket, further demonstrating how large ligands can travel through the pockets within both Mb and Hb to reach the heme active site. The work presented in this chapter thus demonstrates a wide range of products that can result from the reaction of Mb and Hb with nitro- and hydroxylamine-containing compounds. In Chapter 3, the focus was on C. difficile NRs responsible for metabolizing the antibiotic Mtz. Using UV-vis spectroscopy, I confirmed that a putative NR from C. difficile does in fact function as a Type I NR. Additionally, I solved its X-ray crystal structure, one of the first two reported from the hypervirulent C. difficile strain. The X-ray crystal structure also revealed a putative binding site for Mtz. The work in this chapter provides one of the first expression, purification, characterization and crystallization of a NR from the hypervirulent C. difficile strain. The focus of Chapter 4 was on the interaction of cytochrome P450 BM3-HD with RNOs, imidazoles and arylhydrazines. Using spectroscopy, I showed that the interaction of RNOs with P450 BM3-HD result in N-bound products and the extent of product formation was dependent on alkyl group size. Imidazoles were found to bind through their N-atoms in a type II fashion. And finally, arylhydrazines were observed to initially bind in a type II manner, but with exposure to air, they formed sigma-bonded aryl-iron complexes. The work in this chapter elucidates the identity of the products in the reaction of P450 BM3-HD with RNOs, imidazoles and arylhydrazines. Together, the work presented in Chapters 2-4, shows how N-containing compounds and… Advisors/Committee Members: Addo%2C%20George%20B.%22%29&pagesize-30">Richter-Addo, George B. (advisor), West, Ann H. (committee member), Bourne, Christina (committee member), Duerfeldt, Adam (committee member), Dunn, Anne K. (committee member).

Subjects/Keywords: structural biology; nitroreductase; cytochrome P450; nitrogen compounds; heme proteins

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APA (6^th Edition):

Powell, S. M. (2019). THE STRUCTURAL CHARACTERIZATION OF THE INTERACTIONS OF MYOGLOBIN, HEMOGLOBIN, C. DIFFICILE NITROREDUCTASE AND CYTOCHROME P450 WITH N-CONTAINING COMPOUNDS. (Doctoral Dissertation). University of Oklahoma. Retrieved from http://hdl.handle.net/11244/319369

Chicago Manual of Style (16^th Edition):

Powell, Samantha M. “THE STRUCTURAL CHARACTERIZATION OF THE INTERACTIONS OF MYOGLOBIN, HEMOGLOBIN, C. DIFFICILE NITROREDUCTASE AND CYTOCHROME P450 WITH N-CONTAINING COMPOUNDS.” 2019. Doctoral Dissertation, University of Oklahoma. Accessed February 28, 2021. http://hdl.handle.net/11244/319369.

MLA Handbook (7^th Edition):

Powell, Samantha M. “THE STRUCTURAL CHARACTERIZATION OF THE INTERACTIONS OF MYOGLOBIN, HEMOGLOBIN, C. DIFFICILE NITROREDUCTASE AND CYTOCHROME P450 WITH N-CONTAINING COMPOUNDS.” 2019. Web. 28 Feb 2021.

Vancouver:

Powell SM. THE STRUCTURAL CHARACTERIZATION OF THE INTERACTIONS OF MYOGLOBIN, HEMOGLOBIN, C. DIFFICILE NITROREDUCTASE AND CYTOCHROME P450 WITH N-CONTAINING COMPOUNDS. [Internet] [Doctoral dissertation]. University of Oklahoma; 2019. [cited 2021 Feb 28]. Available from: http://hdl.handle.net/11244/319369.

Council of Science Editors:

Powell SM. THE STRUCTURAL CHARACTERIZATION OF THE INTERACTIONS OF MYOGLOBIN, HEMOGLOBIN, C. DIFFICILE NITROREDUCTASE AND CYTOCHROME P450 WITH N-CONTAINING COMPOUNDS. [Doctoral Dissertation]. University of Oklahoma; 2019. Available from: http://hdl.handle.net/11244/319369

University of Oklahoma

3. Guan, Ye. REACTIONS OF NITRIC OXIDE, NITROSOALKANES WITH GROUP 8 & 9 METALLOPORPHYRINS AND HEME PROTEINS.

Degree: PhD, 2015, University of Oklahoma

URL: http://hdl.handle.net/11244/15493

► This dissertation describes the interactions of nitric oxide (NO) and C-nitrosoalkanes (RNO) with group 8 and 9 metalloporphyrins and heme proteins. The goal of this… (more)

Subjects/Keywords: Chemistry; inorganic; biochemistry

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APA (6^th Edition):

Guan, Y. (2015). REACTIONS OF NITRIC OXIDE, NITROSOALKANES WITH GROUP 8 & 9 METALLOPORPHYRINS AND HEME PROTEINS. (Doctoral Dissertation). University of Oklahoma. Retrieved from http://hdl.handle.net/11244/15493

Chicago Manual of Style (16^th Edition):

Guan, Ye. “REACTIONS OF NITRIC OXIDE, NITROSOALKANES WITH GROUP 8 & 9 METALLOPORPHYRINS AND HEME PROTEINS.” 2015. Doctoral Dissertation, University of Oklahoma. Accessed February 28, 2021. http://hdl.handle.net/11244/15493.

MLA Handbook (7^th Edition):

Guan, Ye. “REACTIONS OF NITRIC OXIDE, NITROSOALKANES WITH GROUP 8 & 9 METALLOPORPHYRINS AND HEME PROTEINS.” 2015. Web. 28 Feb 2021.

Vancouver:

Guan Y. REACTIONS OF NITRIC OXIDE, NITROSOALKANES WITH GROUP 8 & 9 METALLOPORPHYRINS AND HEME PROTEINS. [Internet] [Doctoral dissertation]. University of Oklahoma; 2015. [cited 2021 Feb 28]. Available from: http://hdl.handle.net/11244/15493.

Council of Science Editors:

Guan Y. REACTIONS OF NITRIC OXIDE, NITROSOALKANES WITH GROUP 8 & 9 METALLOPORPHYRINS AND HEME PROTEINS. [Doctoral Dissertation]. University of Oklahoma; 2015. Available from: http://hdl.handle.net/11244/15493

University of Oklahoma

4. Hebdon, Skyler D. Determinants of gene targeting and regulation by response regulators in Clostridioides difficile.

Degree: PhD, 2018, University of Oklahoma

URL: http://hdl.handle.net/11244/316297

► Bacteria use two-component signal transduction systems to sense the conditions of the environment and adapt their behavior to ensure survival. The separate roles of signal… (more)

▼ Bacteria use two-component signal transduction systems to sense the conditions of the environment and adapt their behavior to ensure survival. The separate roles of signal perception and response output are carried out by histidine kinase and response regulator proteins, respectively. Most response regulators alter gene transcription, but it is not yet possible to predict which genes they regulate. The precise prediction of these gene regulatory outputs could enable researchers to predict, and doctors and patients to mitigate, various bacterial behaviors. This dissertation presents the elucidation of the genes and biological functions regulated by two response regulators, RR_1586 and RR_1677, from the hypervirulent human pathogen Clostridioides difficile R20291. The data presented herein supports the conclusion that RR_1586 regulates genes involved in phosphate transport, and further characterization of its activity suggests several mechanisms it uses to regulate those genes. The bacterial one-hybrid assay used in this study to elucidate the gene regulatory targets of RR_1586 could potentially be used to find a generalizable solution to predicting gene targets of all response regulators from genome sequences alone. In the process of optimizing the bacterial one-hybrid assay for such a broadly impactful endeavor, it was found that RR_1677 appears to regulate the processes of protein synthesis and cell wall synthesis. A bioinformatics pipeline was also constructed by combining several existing utilities to analyze and interpret the experimental results. Two additional lines of research are also presented. The first is the adaptation of Fourier-transform infrared spectroscopy to observe response regulator phosphorylation. This method offers an alternative from the more labor-intensive methods currently available. The second is an analysis of the biophysical interactions between a response regulator from Saccharomyces cerevisiae and its binding partner, a histidine-containing phosphotransfer protein. Characterization of this interaction elucidates the physical impetus behind the evolutionary conservation of a specific glycine residue near the active site whose role was previously unknown. Advisors/Committee Members: West, Ann. H (advisor), Addo%2C%20George%20B.%22%29&pagesize-30">Richter-Addo, George B. (committee member), Bourne, Christina (committee member), Karr, Elizabeth A. (committee member), Yip, Ivan (committee member).

Subjects/Keywords: Two-component signal transduction; response regulator; DNA binding; regulon; bioinformatics; Clostridioides difficile

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APA (6^th Edition):

Hebdon, S. D. (2018). Determinants of gene targeting and regulation by response regulators in Clostridioides difficile. (Doctoral Dissertation). University of Oklahoma. Retrieved from http://hdl.handle.net/11244/316297

Chicago Manual of Style (16^th Edition):

Hebdon, Skyler D. “Determinants of gene targeting and regulation by response regulators in Clostridioides difficile.” 2018. Doctoral Dissertation, University of Oklahoma. Accessed February 28, 2021. http://hdl.handle.net/11244/316297.

MLA Handbook (7^th Edition):

Hebdon, Skyler D. “Determinants of gene targeting and regulation by response regulators in Clostridioides difficile.” 2018. Web. 28 Feb 2021.

Vancouver:

Hebdon SD. Determinants of gene targeting and regulation by response regulators in Clostridioides difficile. [Internet] [Doctoral dissertation]. University of Oklahoma; 2018. [cited 2021 Feb 28]. Available from: http://hdl.handle.net/11244/316297.

Council of Science Editors:

Hebdon SD. Determinants of gene targeting and regulation by response regulators in Clostridioides difficile. [Doctoral Dissertation]. University of Oklahoma; 2018. Available from: http://hdl.handle.net/11244/316297

University of Oklahoma

5. Wang, Bing. X-RAY CRYSTAL STRUCTURES AND CHARACTERIZATION OF THE PRODUCTS FROM THE INTERACTIONS OF MYOGLOBIN WITH NITROGEN OXIDES AND ARYLHYDRAZINES, AND NITROREDUCTASE INTERACTIONS WITH ORGANIC NITRO COMPOUNDS.

Degree: PhD, 2016, University of Oklahoma

URL: http://hdl.handle.net/11244/34616

► This thesis describes research into the roles that metalloproteins and non-metalloproteins play in the biological inorganic/organic chemistry of common nitrogen oxides. There are three main… (more)

▼ This thesis describes research into the roles that metalloproteins and non-metalloproteins play in the biological inorganic/organic chemistry of common nitrogen oxides. There are three main chapters on this work: the first details the reactions of wild-type and mutant myoglobins (Mbs) in their interactions with nitrite and nitric oxide (NO), the second deals with these Mbs and their formation of bioorganometallic derivatives when reacted with arylhydrazines, and the third deals with an FMN-dependent nitroreductase enzyme and its reactions with the clinically relevant metronidazole drug. Mutations to the distal pocket in the active site of Mb were made; specifically, ferric-aqua derivatives of the mutants were expressed, purified, crystallized, and their crystal structures solved to 1.78-1.85 Å resolution. The proteins crystallized in either the P21 or P6 space groups. The crystals were soaked with nitrite to form their O-bonded MbIII(ONO) complexes whose structures were also solved to 1.57-1.85 Å resolution. In the case of the H64A distal pocket mutant missing the H-bonding amino-acid residue in the 64th position, a water bridge was observed to form linking the protein exterior with the bound nitrite ligand, thus replacing the expected wt H64 H-bonding feature. Further, we noted that the distal pocket Val68 residue adapted its conformation to accommodate the nitrite ligands in some of these complexes. Notably, the O-binding modes observed in the four wt and mutant structures held up exceedingly well even with the variation in H-bonding capacities. These wt and mutant Mb(ONO) compounds can be reduced with sodium dithionite to their respective nitrosyl Mb(NO) products. Verification of the formation of the nitrosyl Fe-NO derivative, and not the closely related nitroxyl Fe-HNO, was provided by FT-infrared spectroscopy. Arylhydrazines and derivatives are prevalent in nature and in pharmaceutical drugs. They interact with various heme proteins resulting in deactivation of the proteins. Eleven X-ray crystal structures of the products from the reactions of wt and mutant (H64A, H64Q, V68A/I107Y) Mbs with arylhydrazines (ArNHNH2; Ar = Ph, m-tol, and p-chlorophenyl) were obtained to 1.70-1.98 Å resolution. Direct Fe-carbon bonds were observed in all these derivatives, establishing that the hydrazine -NHNH2 moieties had been released from the reagents during their reactions with the Fe centers of the Mbs. Importantly, the C-atoms coordinating to the Fe centers were the same as those that bonded to the hydrazine functional groups, implying that the carbon-based radical intermediates were formed in close proximity to the Fe centers allowing for facile and efficient reactions to give the bioorganometallic Mb-aryl products. Significant distal pocket amino acid movements were observed in some cases with the larger p-chlorophenyl ligand aryl; for example, in the H64Q-chlorophenyl derivative, the Gln64 residue swings to a position outside the pocket towards the solvent region. We report the first expression, purification,… Advisors/Committee Members: Addo%2C%20George%20B.%22%29&pagesize-30">Richter-Addo, George B. (advisor), West, Ann H. (committee member), Nicholas, Kenneth M. (committee member), Li, Jun (committee member), Ruyle, Jessica (committee member).

Subjects/Keywords: crystallography; myoglobin; nitrite; nitric oxide; nitroreductase; metronidazole

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APA (6^th Edition):

Wang, B. (2016). X-RAY CRYSTAL STRUCTURES AND CHARACTERIZATION OF THE PRODUCTS FROM THE INTERACTIONS OF MYOGLOBIN WITH NITROGEN OXIDES AND ARYLHYDRAZINES, AND NITROREDUCTASE INTERACTIONS WITH ORGANIC NITRO COMPOUNDS. (Doctoral Dissertation). University of Oklahoma. Retrieved from http://hdl.handle.net/11244/34616

Chicago Manual of Style (16^th Edition):

Wang, Bing. “X-RAY CRYSTAL STRUCTURES AND CHARACTERIZATION OF THE PRODUCTS FROM THE INTERACTIONS OF MYOGLOBIN WITH NITROGEN OXIDES AND ARYLHYDRAZINES, AND NITROREDUCTASE INTERACTIONS WITH ORGANIC NITRO COMPOUNDS.” 2016. Doctoral Dissertation, University of Oklahoma. Accessed February 28, 2021. http://hdl.handle.net/11244/34616.

MLA Handbook (7^th Edition):

Wang, Bing. “X-RAY CRYSTAL STRUCTURES AND CHARACTERIZATION OF THE PRODUCTS FROM THE INTERACTIONS OF MYOGLOBIN WITH NITROGEN OXIDES AND ARYLHYDRAZINES, AND NITROREDUCTASE INTERACTIONS WITH ORGANIC NITRO COMPOUNDS.” 2016. Web. 28 Feb 2021.

Vancouver:

Wang B. X-RAY CRYSTAL STRUCTURES AND CHARACTERIZATION OF THE PRODUCTS FROM THE INTERACTIONS OF MYOGLOBIN WITH NITROGEN OXIDES AND ARYLHYDRAZINES, AND NITROREDUCTASE INTERACTIONS WITH ORGANIC NITRO COMPOUNDS. [Internet] [Doctoral dissertation]. University of Oklahoma; 2016. [cited 2021 Feb 28]. Available from: http://hdl.handle.net/11244/34616.

Council of Science Editors:

Wang B. X-RAY CRYSTAL STRUCTURES AND CHARACTERIZATION OF THE PRODUCTS FROM THE INTERACTIONS OF MYOGLOBIN WITH NITROGEN OXIDES AND ARYLHYDRAZINES, AND NITROREDUCTASE INTERACTIONS WITH ORGANIC NITRO COMPOUNDS. [Doctoral Dissertation]. University of Oklahoma; 2016. Available from: http://hdl.handle.net/11244/34616

University of Oklahoma

6. Carter, Shawn M. Syntheses, molecular structures, and fiber-optic infrared spectroelectrochemistry of nitrosyl metalloporphyrins containing axially bound alkoxide, thiolate, imidazole, and imidazolate ligands.

Degree: PhD, Department of Chemistry and Biochemistry, 2006, University of Oklahoma

URL: http://hdl.handle.net/11244/1132

► Chapter 1 introduces the fundamental issues involved in the chemistry of Group 8 Fe, Ru, and Os nitrosyl porphyrin complexes with trans and O- and… (more)

Subjects/Keywords: Hemoproteins.; Osmium Spectra.; Electrochemistry.; Ligands.; Ruthenium.; Spectrum analysis.; Chemistry, Inorganic.

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APA (6^th Edition):

Carter, S. M. (2006). Syntheses, molecular structures, and fiber-optic infrared spectroelectrochemistry of nitrosyl metalloporphyrins containing axially bound alkoxide, thiolate, imidazole, and imidazolate ligands. (Doctoral Dissertation). University of Oklahoma. Retrieved from http://hdl.handle.net/11244/1132

Chicago Manual of Style (16^th Edition):

Carter, Shawn M. “Syntheses, molecular structures, and fiber-optic infrared spectroelectrochemistry of nitrosyl metalloporphyrins containing axially bound alkoxide, thiolate, imidazole, and imidazolate ligands.” 2006. Doctoral Dissertation, University of Oklahoma. Accessed February 28, 2021. http://hdl.handle.net/11244/1132.

MLA Handbook (7^th Edition):

Carter, Shawn M. “Syntheses, molecular structures, and fiber-optic infrared spectroelectrochemistry of nitrosyl metalloporphyrins containing axially bound alkoxide, thiolate, imidazole, and imidazolate ligands.” 2006. Web. 28 Feb 2021.

Vancouver:

Carter SM. Syntheses, molecular structures, and fiber-optic infrared spectroelectrochemistry of nitrosyl metalloporphyrins containing axially bound alkoxide, thiolate, imidazole, and imidazolate ligands. [Internet] [Doctoral dissertation]. University of Oklahoma; 2006. [cited 2021 Feb 28]. Available from: http://hdl.handle.net/11244/1132.

Council of Science Editors:

Carter SM. Syntheses, molecular structures, and fiber-optic infrared spectroelectrochemistry of nitrosyl metalloporphyrins containing axially bound alkoxide, thiolate, imidazole, and imidazolate ligands. [Doctoral Dissertation]. University of Oklahoma; 2006. Available from: http://hdl.handle.net/11244/1132

University of Oklahoma

7. Zahran, Zaki Nabeih Ahmed. A bioinorganic approach to the study of the interactions of nitrogen oxides with manganese porphyrins and manganese- and cobalt-reconstituted myoglobin.

Degree: PhD, Department of Chemistry and Biochemistry, 2007, University of Oklahoma

URL: http://hdl.handle.net/11244/1272

► Chapter 3 describes the syntheses of a new set of six-coordinate manganese nitrosyl porphyrins of the general form (por)Mn(NO)(L) (por = TTP, TPP, T( p-OCH3)PP;… (more)

Subjects/Keywords: Nitric oxide.; Porphyrins.; Chemistry, Biochemistry.; Chemistry, Inorganic.; Myoglobin.

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APA (6^th Edition):

Zahran, Z. N. A. (2007). A bioinorganic approach to the study of the interactions of nitrogen oxides with manganese porphyrins and manganese- and cobalt-reconstituted myoglobin. (Doctoral Dissertation). University of Oklahoma. Retrieved from http://hdl.handle.net/11244/1272

Chicago Manual of Style (16^th Edition):

Zahran, Zaki Nabeih Ahmed. “A bioinorganic approach to the study of the interactions of nitrogen oxides with manganese porphyrins and manganese- and cobalt-reconstituted myoglobin.” 2007. Doctoral Dissertation, University of Oklahoma. Accessed February 28, 2021. http://hdl.handle.net/11244/1272.

MLA Handbook (7^th Edition):

Zahran, Zaki Nabeih Ahmed. “A bioinorganic approach to the study of the interactions of nitrogen oxides with manganese porphyrins and manganese- and cobalt-reconstituted myoglobin.” 2007. Web. 28 Feb 2021.

Vancouver:

Zahran ZNA. A bioinorganic approach to the study of the interactions of nitrogen oxides with manganese porphyrins and manganese- and cobalt-reconstituted myoglobin. [Internet] [Doctoral dissertation]. University of Oklahoma; 2007. [cited 2021 Feb 28]. Available from: http://hdl.handle.net/11244/1272.

Council of Science Editors:

Zahran ZNA. A bioinorganic approach to the study of the interactions of nitrogen oxides with manganese porphyrins and manganese- and cobalt-reconstituted myoglobin. [Doctoral Dissertation]. University of Oklahoma; 2007. Available from: http://hdl.handle.net/11244/1272

University of Oklahoma

8. Xu, Nan. Interactions of nitric oxide and nitrosamines with group 8 metalloporphyrins.

Degree: PhD, Department of Chemistry and Biochemistry, 2007, University of Oklahoma

URL: http://hdl.handle.net/11244/1314

This dissertation describes the interactions of nitric oxide and nitrosamines with group 8 metalloporphyrins. Advisors/Committee Members: Richter-Addo, George B., (advisor).

Subjects/Keywords: Hemoproteins.; Nitrosoamines.; Chemistry, Inorganic.; Porphyrins.; Nitric oxide.

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

APA (6^th Edition):

Xu, N. (2007). Interactions of nitric oxide and nitrosamines with group 8 metalloporphyrins. (Doctoral Dissertation). University of Oklahoma. Retrieved from http://hdl.handle.net/11244/1314

Chicago Manual of Style (16^th Edition):

Xu, Nan. “Interactions of nitric oxide and nitrosamines with group 8 metalloporphyrins.” 2007. Doctoral Dissertation, University of Oklahoma. Accessed February 28, 2021. http://hdl.handle.net/11244/1314.

MLA Handbook (7^th Edition):

Xu, Nan. “Interactions of nitric oxide and nitrosamines with group 8 metalloporphyrins.” 2007. Web. 28 Feb 2021.

Vancouver:

Xu N. Interactions of nitric oxide and nitrosamines with group 8 metalloporphyrins. [Internet] [Doctoral dissertation]. University of Oklahoma; 2007. [cited 2021 Feb 28]. Available from: http://hdl.handle.net/11244/1314.

Council of Science Editors:

Xu N. Interactions of nitric oxide and nitrosamines with group 8 metalloporphyrins. [Doctoral Dissertation]. University of Oklahoma; 2007. Available from: http://hdl.handle.net/11244/1314

University of Oklahoma

9. Chen, Li. Nitrosyl and nitroso complexes of group 8 metalloporphyrins.

Degree: PhD, Department of Chemistry and Biochemistry, 1998, University of Oklahoma

URL: http://hdl.handle.net/11244/5650

► Chapter 1 of this dissertation describes the formal trans addition of thionitrites (RSNO) and alkyl nitrites (RONO) to Os^II porphyrins, and the investigation of… (more)

Subjects/Keywords: Chemistry, Organic.; Nitroso compounds.; Porphyrins.

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

APA (6^th Edition):

Chen, L. (1998). Nitrosyl and nitroso complexes of group 8 metalloporphyrins. (Doctoral Dissertation). University of Oklahoma. Retrieved from http://hdl.handle.net/11244/5650

Chicago Manual of Style (16^th Edition):

Chen, Li. “Nitrosyl and nitroso complexes of group 8 metalloporphyrins.” 1998. Doctoral Dissertation, University of Oklahoma. Accessed February 28, 2021. http://hdl.handle.net/11244/5650.

MLA Handbook (7^th Edition):

Chen, Li. “Nitrosyl and nitroso complexes of group 8 metalloporphyrins.” 1998. Web. 28 Feb 2021.

Vancouver:

Chen L. Nitrosyl and nitroso complexes of group 8 metalloporphyrins. [Internet] [Doctoral dissertation]. University of Oklahoma; 1998. [cited 2021 Feb 28]. Available from: http://hdl.handle.net/11244/5650.

Council of Science Editors:

Chen L. Nitrosyl and nitroso complexes of group 8 metalloporphyrins. [Doctoral Dissertation]. University of Oklahoma; 1998. Available from: http://hdl.handle.net/11244/5650

University of Oklahoma

10. Lee, Jonghyuk. Interactions of organic S-nitroso and C-nitroso compounds with metalloporphyrins.

Degree: PhD, Department of Chemistry and Biochemistry, 2002, University of Oklahoma

URL: http://hdl.handle.net/11244/497

This dissertation deals with the interactions of organic S-nitroso (RS-N=0) and C-nitroso (C-N=0) compounds with ruthenium and osmium porphyrins. Advisors/Committee Members: Richter-Addo, George B., (advisor).

Subjects/Keywords: Chemistry, Inorganic.; Nitroso compounds.; Porphyrins.; Nitrogen compounds.

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APA (6^th Edition):

Lee, J. (2002). Interactions of organic S-nitroso and C-nitroso compounds with metalloporphyrins. (Doctoral Dissertation). University of Oklahoma. Retrieved from http://hdl.handle.net/11244/497

Chicago Manual of Style (16^th Edition):

Lee, Jonghyuk. “Interactions of organic S-nitroso and C-nitroso compounds with metalloporphyrins.” 2002. Doctoral Dissertation, University of Oklahoma. Accessed February 28, 2021. http://hdl.handle.net/11244/497.

MLA Handbook (7^th Edition):

Lee, Jonghyuk. “Interactions of organic S-nitroso and C-nitroso compounds with metalloporphyrins.” 2002. Web. 28 Feb 2021.

Vancouver:

Lee J. Interactions of organic S-nitroso and C-nitroso compounds with metalloporphyrins. [Internet] [Doctoral dissertation]. University of Oklahoma; 2002. [cited 2021 Feb 28]. Available from: http://hdl.handle.net/11244/497.

Council of Science Editors:

Lee J. Interactions of organic S-nitroso and C-nitroso compounds with metalloporphyrins. [Doctoral Dissertation]. University of Oklahoma; 2002. Available from: http://hdl.handle.net/11244/497

University of Oklahoma

11. Jones, Myron Wayne. Fiber-Optic Infrared Spectroelectrochemistry of Some Dinitrosyl Iron Phosphine Complexes and an NMR Kinetics and Equilibrium Study of an Organic Nitroso Compound in Various Solvents.

Degree: PhD, 2010, University of Oklahoma

URL: http://hdl.handle.net/11244/319209

► Chapter 3 describes the study of a C-nitroso compound, namely the dimeric 2-methyl-2-nitrosopropane, in various solvents. Interest in the fundamental properties of C-nitroso compounds has… (more)

Subjects/Keywords: Phosphine; Ligands; Nitroso compounds; Spectrum analysis; Electrochemistry

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

APA (6^th Edition):

Jones, M. W. (2010). Fiber-Optic Infrared Spectroelectrochemistry of Some Dinitrosyl Iron Phosphine Complexes and an NMR Kinetics and Equilibrium Study of an Organic Nitroso Compound in Various Solvents. (Doctoral Dissertation). University of Oklahoma. Retrieved from http://hdl.handle.net/11244/319209

Chicago Manual of Style (16^th Edition):

Jones, Myron Wayne. “Fiber-Optic Infrared Spectroelectrochemistry of Some Dinitrosyl Iron Phosphine Complexes and an NMR Kinetics and Equilibrium Study of an Organic Nitroso Compound in Various Solvents.” 2010. Doctoral Dissertation, University of Oklahoma. Accessed February 28, 2021. http://hdl.handle.net/11244/319209.

MLA Handbook (7^th Edition):

Jones, Myron Wayne. “Fiber-Optic Infrared Spectroelectrochemistry of Some Dinitrosyl Iron Phosphine Complexes and an NMR Kinetics and Equilibrium Study of an Organic Nitroso Compound in Various Solvents.” 2010. Web. 28 Feb 2021.

Vancouver:

Jones MW. Fiber-Optic Infrared Spectroelectrochemistry of Some Dinitrosyl Iron Phosphine Complexes and an NMR Kinetics and Equilibrium Study of an Organic Nitroso Compound in Various Solvents. [Internet] [Doctoral dissertation]. University of Oklahoma; 2010. [cited 2021 Feb 28]. Available from: http://hdl.handle.net/11244/319209.

Council of Science Editors:

Jones MW. Fiber-Optic Infrared Spectroelectrochemistry of Some Dinitrosyl Iron Phosphine Complexes and an NMR Kinetics and Equilibrium Study of an Organic Nitroso Compound in Various Solvents. [Doctoral Dissertation]. University of Oklahoma; 2010. Available from: http://hdl.handle.net/11244/319209

University of Oklahoma

12. Copeland, Daniel Morris. A study of the interactions of nitric oxide and nitric oxide containing molecules with heme proteins.

Degree: PhD, Department of Chemistry and Biochemistry, 2006, University of Oklahoma

URL: http://hdl.handle.net/11244/1101

► Recently, it has been shown that hemoglobin (Hb) and myoglobin catalyze the reduction of nitrite to NO under hypoxic conditions. Prior to our work, there… (more)

Subjects/Keywords: Hemoproteins.; Nitric oxide.; Myoglobin.; Chemistry, Inorganic.; Chemistry, Biochemistry.

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

APA (6^th Edition):

Copeland, D. M. (2006). A study of the interactions of nitric oxide and nitric oxide containing molecules with heme proteins. (Doctoral Dissertation). University of Oklahoma. Retrieved from http://hdl.handle.net/11244/1101

Chicago Manual of Style (16^th Edition):

Copeland, Daniel Morris. “A study of the interactions of nitric oxide and nitric oxide containing molecules with heme proteins.” 2006. Doctoral Dissertation, University of Oklahoma. Accessed February 28, 2021. http://hdl.handle.net/11244/1101.

MLA Handbook (7^th Edition):

Copeland, Daniel Morris. “A study of the interactions of nitric oxide and nitric oxide containing molecules with heme proteins.” 2006. Web. 28 Feb 2021.

Vancouver:

Copeland DM. A study of the interactions of nitric oxide and nitric oxide containing molecules with heme proteins. [Internet] [Doctoral dissertation]. University of Oklahoma; 2006. [cited 2021 Feb 28]. Available from: http://hdl.handle.net/11244/1101.

Council of Science Editors:

Copeland DM. A study of the interactions of nitric oxide and nitric oxide containing molecules with heme proteins. [Doctoral Dissertation]. University of Oklahoma; 2006. Available from: http://hdl.handle.net/11244/1101

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