Journal article icon

Journal article

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 open...

Expand abstract

Actions


Access Document


Publisher copy:
10.1016/j.jmb.2012.03.022

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Physics
Role:
Author
Expand authors...
Journal:
Journal of molecular biology
Volume:
420
Issue:
4-5
Pages:
296-309
Publication date:
2012-07-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:079315d3-e2e1-46a9-9536-8ab08cbf5298
Source identifiers:
329065
Local pid:
pubs:329065

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP