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The closed and compact domain organization of the 70-kDa human cytochrome P450 reductase in its oxidized state as revealed by NMR

Abstract:

The NADPH cytochrome P450 reductase (CPR), a diflavin enzyme, catalyzes the electron transfer (ET) from NADPH to the substrate P450. The crystal structures of mammalian and yeast CPRs show a compact organization for the two domains containing FMN (flavin mononucleotide) and FAD (flavin adenine dinucleotide), with a short interflavin distance consistent with fast ET from the NADPH-reduced FAD to the second flavin FMN. This conformation, referred as closed, contrasts with the alternative opened...

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Publisher copy:
10.1016/j.jmb.2012.03.022

Authors


Vincent, B More by this author
Morellet, N More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Physics
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Journal:
Journal of Molecular Biology
Volume:
420
Issue:
4-5
Pages:
296-309
Publication date:
2012-07-20
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:7ba9a6bb-f196-4c1e-9da1-504a9811e09d
Source identifiers:
340235
Local pid:
pubs:340235

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