- 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 - Publisher copy:
- 10.1016/j.jmb.2012.03.022
-
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- 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
- Copyright date:
- 2012
Journal article
The closed and compact domain organization of the 70-kDa human cytochrome P450 reductase in its oxidized state as revealed by NMR.
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