Resolution and reconstitution of the NADPH-cytochrome c (P-450) reductase induced by progesterone in Rhizopus nigricans.
The NADPH-cytochrome c (P-450) reductase induced in the filamentous fungus Rhizopus nigricans as a component of 11 alpha-hydroxylase of progesterone was resolved by DEAE-cellulose chromatography into two components. One of the components is an iron-sulfur protein (rhizoporedoxin), whereas the other component is a protein with reductase activity dependent on NADPH (rhizoporedoxin reductase). As shown in the reconstitution assay, the NADPH-cytochrome c (P-450) reductase activity was restored upon combination of these two proteins.
D002021:Buffers; D002848:Chromatography, DEAE-Cellulose; D004790:Enzyme Induction / Q000187:drug effects; D007506:Iron-Sulfur Proteins / Q000302:isolation & purification; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology; D009252:NADPH Dehydrogenase / Q000302:isolation & purification; D009251:NADPH-Ferrihemoprotein Reductase / Q000096:biosynthesis / Q000302:isolation & purification*; D011374:Progesterone / Q000494:pharmacology*; D012233:Rhizopus / Q000201:enzymology*
D002021:Buffers; D007506:Iron-Sulfur Proteins; D011374:Progesterone; D009251:NADPH-Ferrihemoprotein Reductase; D009252:NADPH Dehydrogenase