Title : A well-balanced preexisting equilibrium governs electron flux efficiency of a multidomain diflavin reductase.

Pub. Date : 2015 Mar 24

PMID : 25809265






2 Functional Relationships(s)
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1 Using small-angle x-ray scattering and nuclear magnetic resonance data, we describe the conformational free-energy landscape of the NADPH-cytochrome P450 reductase (CPR), a typical bidomain redox enzyme composed of two covalently-bound flavin domains, under various experimental conditions. 4,6-dinitro-o-cresol cytochrome p450 oxidoreductase Homo sapiens
2 Using small-angle x-ray scattering and nuclear magnetic resonance data, we describe the conformational free-energy landscape of the NADPH-cytochrome P450 reductase (CPR), a typical bidomain redox enzyme composed of two covalently-bound flavin domains, under various experimental conditions. 4,6-dinitro-o-cresol cytochrome p450 oxidoreductase Homo sapiens