Functional Characterization of the re-Face Loop Spanning Residues 536−541 and Its Interactions with the Cofactor in the Flavin Mononucleotide-Binding Domain of Flavocytochrome P450 from Bacillus megaterium-Reference-Cited by-同舟云学术

Functional Characterization of the re-Face Loop Spanning Residues 536−541 and Its Interactions with the Cofactor in the Flavin Mononucleotide-Binding Domain of Flavocytochrome P450 from Bacillus megaterium

Published:2009-05-26 Issue:23 Volume:48 Page:5131-5141
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kasim Mumtaz¹,Chen Huai-Chun¹,Swenson Richard P.¹

Affiliation:

1. Department of Biochemistry and Ohio State Biochemistry Program, The Ohio State University, Columbus, Ohio 43210

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi900607q

Reference54 articles.

1. Protein engineering of cytochromes P-450

2. Coding Nucleotide, 5′ Regulatory, and Deduced Amino Acid Sequences of P-450BM-3, a Single Peptide Cytochrome P-450:NADPH-P-450 Reductase from Bacillus megaterium

3. Structure of a cytochrome P450-redox partner electron-transfer complex

4. Equilibrium and Transient State Spectrophotometric Studies of the Mechanism of Reduction of the Flavoprotein Domain of P450BM-3

5. Redox Control of the Catalytic Cycle of Flavocytochrome P-450 BM3

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