Resolution and reconstitution of cytochrome P-450 containing steroid hydroxylation system of Rhizopus nigricans.
11 alpha-hydroxylation of progesterone in the eucaryotic filamentous fungus Rhizopus nigricans is catalyzed by a monooxygenase. Three components of this multienzyme system, cytochrome P-450, rhizoporedoxin and a FAD containing rhizoporedoxin reductase have been separated from the postmitochondrial fraction on DEAE cellulose. Using NADPH as electron donor we showed that the presence of all three components was necessary for the reconstitution of the active electron transport chain.
D003577:Cytochrome P-450 Enzyme System / Q000032:analysis*; D004579:Electron Transport; D006900:Hydroxylation; D009249:NADP / Q000378:metabolism; D012233:Rhizopus / Q000201:enzymology*; D013250:Steroid Hydroxylases / Q000032:analysis*
D009249:NADP; D003577:Cytochrome P-450 Enzyme System; D013250:Steroid Hydroxylases; C074514:steroid 11-alpha-hydroxylase