Title : Conformational changes of NADPH-cytochrome P450 oxidoreductase are essential for catalysis and cofactor binding.

Pub. Date : 2011 May 6

PMID : 21345800






1 Functional Relationships(s)
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1 Furthermore, comparison of these mutant and wild type structures strongly suggests that the Gly(631)-Asn(635) loop movement controls NADPH binding and NADP(+) release; this loop movement in turn facilitates the flavin domain movement, allowing electron transfer from FMN to the CYPOR redox partners. 4,6-dinitro-o-cresol cytochrome p450 oxidoreductase Homo sapiens