Conformational Changes of NADPH-Cytochrome P450 Oxidoreductase Are Essential for Catalysis and Cofactor Binding

The crystal structure of NADPH-cytochrome P450 reductase (CYPOR) implies that a large domain movement is essential for electron transfer from NADPH via FAD and FMN to its redox partners. To test this hypothesis, a disulfide bond was engineered between residues Asp(147) and Arg(514) in the FMN and FA...

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Hlavní autoři: Xia, Chuanwu, Hamdane, Djemel, Shen, Anna L., Choi, Vivian, Kasper, Charles B., Pearl, Naw May, Zhang, Haoming, Im, Sang-Choul, Waskell, Lucy, Kim, Jung-Ja P.
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2011
Témata:
Enzymology
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3091232/
https://ncbi.nlm.nih.gov/pubmed/21345800
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.230532
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