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You searched for subject:( redox cofactor). Showing records 1 – 4 of 4 total matches.

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The Ohio State University

1. Chen, Huai-Chun. Redox and functional characterization of a surface loop spanning residues 536 to 541 in the flavin mononucleotide-binding domain of flavocytochrome P450BM-3 from Bacillus megaterium.

Degree: PhD, Ohio State Biochemistry Program, 2009, The Ohio State University

 Flavocytochrome P450BM-3 (BM3) displays many of the same characteristics as the mammalian microsomal cytochrome P450 system; however, the two diflavin reductases utilize different electron transfer… (more)

Subjects/Keywords: Biochemistry; flavin; cofactor; redox potential; electron transfer; P450BM-3; flavoprotein

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APA (6th Edition):

Chen, H. (2009). Redox and functional characterization of a surface loop spanning residues 536 to 541 in the flavin mononucleotide-binding domain of flavocytochrome P450BM-3 from Bacillus megaterium. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1236370042

Chicago Manual of Style (16th Edition):

Chen, Huai-Chun. “Redox and functional characterization of a surface loop spanning residues 536 to 541 in the flavin mononucleotide-binding domain of flavocytochrome P450BM-3 from Bacillus megaterium.” 2009. Doctoral Dissertation, The Ohio State University. Accessed October 18, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=osu1236370042.

MLA Handbook (7th Edition):

Chen, Huai-Chun. “Redox and functional characterization of a surface loop spanning residues 536 to 541 in the flavin mononucleotide-binding domain of flavocytochrome P450BM-3 from Bacillus megaterium.” 2009. Web. 18 Oct 2019.

Vancouver:

Chen H. Redox and functional characterization of a surface loop spanning residues 536 to 541 in the flavin mononucleotide-binding domain of flavocytochrome P450BM-3 from Bacillus megaterium. [Internet] [Doctoral dissertation]. The Ohio State University; 2009. [cited 2019 Oct 18]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1236370042.

Council of Science Editors:

Chen H. Redox and functional characterization of a surface loop spanning residues 536 to 541 in the flavin mononucleotide-binding domain of flavocytochrome P450BM-3 from Bacillus megaterium. [Doctoral Dissertation]. The Ohio State University; 2009. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1236370042


Princeton University

2. Liu, Ling. Quantitative analysis of redox metabolism .

Degree: PhD, 2018, Princeton University

 The redox cofactor nicotinamide adenine dinucleotide (NAD) plays a significant role in metabolism and is a substrate for signaling enzymes including poly-ADP-ribose-polymerases (PARPs) and sirtuins.… (more)

Subjects/Keywords: flux quantification; mass spectrometry; metabolism; NAD; NADPH; redox cofactor

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APA (6th Edition):

Liu, L. (2018). Quantitative analysis of redox metabolism . (Doctoral Dissertation). Princeton University. Retrieved from http://arks.princeton.edu/ark:/88435/dsp01js956j498

Chicago Manual of Style (16th Edition):

Liu, Ling. “Quantitative analysis of redox metabolism .” 2018. Doctoral Dissertation, Princeton University. Accessed October 18, 2019. http://arks.princeton.edu/ark:/88435/dsp01js956j498.

MLA Handbook (7th Edition):

Liu, Ling. “Quantitative analysis of redox metabolism .” 2018. Web. 18 Oct 2019.

Vancouver:

Liu L. Quantitative analysis of redox metabolism . [Internet] [Doctoral dissertation]. Princeton University; 2018. [cited 2019 Oct 18]. Available from: http://arks.princeton.edu/ark:/88435/dsp01js956j498.

Council of Science Editors:

Liu L. Quantitative analysis of redox metabolism . [Doctoral Dissertation]. Princeton University; 2018. Available from: http://arks.princeton.edu/ark:/88435/dsp01js956j498


University of South Carolina

3. Dlouhy, Adrian Colleen. Illuminating the Interactions and Functions of Glutaredoxins, BolA Proteins, and Erv1 in Iron Homeostasis.

Degree: PhD, Chemistry and Biochemistry, 2015, University of South Carolina

  Iron is a redox-active protein cofactor required for essential cellular functions such as respiration, however excess intracellular iron can generate damaging reactive oxygen species.… (more)

Subjects/Keywords: Chemistry; Physical Sciences and Mathematics; iron; redox-active protein cofactor; cellular function; Glutaredoxins; iron-sulfur cluster; BolA

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APA (6th Edition):

Dlouhy, A. C. (2015). Illuminating the Interactions and Functions of Glutaredoxins, BolA Proteins, and Erv1 in Iron Homeostasis. (Doctoral Dissertation). University of South Carolina. Retrieved from https://scholarcommons.sc.edu/etd/3193

Chicago Manual of Style (16th Edition):

Dlouhy, Adrian Colleen. “Illuminating the Interactions and Functions of Glutaredoxins, BolA Proteins, and Erv1 in Iron Homeostasis.” 2015. Doctoral Dissertation, University of South Carolina. Accessed October 18, 2019. https://scholarcommons.sc.edu/etd/3193.

MLA Handbook (7th Edition):

Dlouhy, Adrian Colleen. “Illuminating the Interactions and Functions of Glutaredoxins, BolA Proteins, and Erv1 in Iron Homeostasis.” 2015. Web. 18 Oct 2019.

Vancouver:

Dlouhy AC. Illuminating the Interactions and Functions of Glutaredoxins, BolA Proteins, and Erv1 in Iron Homeostasis. [Internet] [Doctoral dissertation]. University of South Carolina; 2015. [cited 2019 Oct 18]. Available from: https://scholarcommons.sc.edu/etd/3193.

Council of Science Editors:

Dlouhy AC. Illuminating the Interactions and Functions of Glutaredoxins, BolA Proteins, and Erv1 in Iron Homeostasis. [Doctoral Dissertation]. University of South Carolina; 2015. Available from: https://scholarcommons.sc.edu/etd/3193


University of Canterbury

4. Greening C. Cofactor Tail Length Modulates Catalysis of Bacterial F420-Dependent Oxidoreductases.

Degree: 2017, University of Canterbury

 F420 is a microbial cofactor that mediates a wide range of physiologically important and industrially relevant redox reactions, including in methanogenesis and tetracycline biosynthesis. This… (more)

Subjects/Keywords: F420; redox; biocatalysis; biodegradation; mycobacterium; actinobacteria; cofactor; Field of Research::06 - Biological Sciences::0601 - Biochemistry and Cell Biology::060101 - Analytical Biochemistry; Field of Research::03 - Chemical Sciences::0304 - Medicinal and Biomolecular Chemistry::030401 - Biologically Active Molecules; Field of Research::10 - Technology::1003 - Industrial Biotechnology::100301 - Biocatalysis and Enzyme Technology; Field of Research::06 - Biological Sciences::0605 - Microbiology::060501 - Bacteriology

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

APA (6th Edition):

C, G. (2017). Cofactor Tail Length Modulates Catalysis of Bacterial F420-Dependent Oxidoreductases. (Thesis). University of Canterbury. Retrieved from http://hdl.handle.net/10092/15164

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

Chicago Manual of Style (16th Edition):

C, Greening. “Cofactor Tail Length Modulates Catalysis of Bacterial F420-Dependent Oxidoreductases.” 2017. Thesis, University of Canterbury. Accessed October 18, 2019. http://hdl.handle.net/10092/15164.

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

MLA Handbook (7th Edition):

C, Greening. “Cofactor Tail Length Modulates Catalysis of Bacterial F420-Dependent Oxidoreductases.” 2017. Web. 18 Oct 2019.

Vancouver:

C G. Cofactor Tail Length Modulates Catalysis of Bacterial F420-Dependent Oxidoreductases. [Internet] [Thesis]. University of Canterbury; 2017. [cited 2019 Oct 18]. Available from: http://hdl.handle.net/10092/15164.

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

Council of Science Editors:

C G. Cofactor Tail Length Modulates Catalysis of Bacterial F420-Dependent Oxidoreductases. [Thesis]. University of Canterbury; 2017. Available from: http://hdl.handle.net/10092/15164

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

.