Ontology highlight
ABSTRACT:
SUBMITTER: Huang WC
PROVIDER: S-EPMC3763376 | biostudies-literature | 2013 Sep
REPOSITORIES: biostudies-literature
Huang Wei-Cheng WC Ellis Jacqueline J Moody Peter C E PC Raven Emma L EL Roberts Gordon C K GC
Structure (London, England : 1993) 20130801 9
NADPH-cytochrome P450 reductase is a key component of the P450 mono-oxygenase drug-metabolizing system. There is evidence for a conformational equilibrium involving large-scale domain motions in this enzyme. We now show, using small-angle X-ray scattering (SAXS) and small-angle neutron scattering, that delivery of two electrons to cytochrome P450 reductase leads to a shift in this equilibrium from a compact form, similar to the crystal structure, toward an extended form, while coenzyme binding f ...[more]