Modification of carboxyl groups on NADPH-cytochrome P-450 reductase involved in binding of cytochromes c and P-450 LM2.
Copyright policy )Modification of carboxyl groups on NADPH-cytochrome P-450 reductase involved in binding of cytochromes c and P-450 LM2.
Carboxyl groups of NADPH-cytochrome P-450 reductase have been modified with the water-soluble carbodiimide EDC. Although there is no significant loss in DCPIP reduction the activity with cytochrome c and cytochrome P-450 LM2 as electron acceptors was inhibited by about 60 and 85%, respectively (1 h incubation time, 20 mM EDC). The inactivation by EDC was nearly completely prevented in the presence of cytochrome P-450 LM2, but not by bovine serum albumin. These results and crosslinking studies suggest that carboxyl groups of NADPH-cytochrome P-450 reductase are involved in charge-pair interactions to cytochrome c and to at least two amino groups of cytochrome P-450 LM2.
Male, Binding Sites, Cytochrome c Group, Serum Albumin, Bovine, Carbodiimides, Cytochrome P-450 Enzyme System, Ethyldimethylaminopropyl Carbodiimide, Animals, Rabbits, Oxidation-Reduction, NADPH-Ferrihemoprotein Reductase
Male, Binding Sites, Cytochrome c Group, Serum Albumin, Bovine, Carbodiimides, Cytochrome P-450 Enzyme System, Ethyldimethylaminopropyl Carbodiimide, Animals, Rabbits, Oxidation-Reduction, NADPH-Ferrihemoprotein Reductase
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