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.
Bernhardt
R
R
Department of Biocatalysis, Academy of Sciences of the GDR, Berlin.
Pommerening
K
K
Ruckpaul
K
K
D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D002234:Carbodiimides / Q000494:pharmacology*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D003574:Cytochrome c Group / Q000378:metabolism*; D005022:Ethyldimethylaminopropyl Carbodiimide / Q000494:pharmacology*; D008297:Male; D009251:NADPH-Ferrihemoprotein Reductase / Q000037:antagonists & inhibitors*; D010084:Oxidation-Reduction; D011817:Rabbits; D012710:Serum Albumin, Bovine / Q000494:pharmacology
D002234:Carbodiimides; D003574:Cytochrome c Group; D012710:Serum Albumin, Bovine; D003577:Cytochrome P-450 Enzyme System; D009251:NADPH-Ferrihemoprotein Reductase; D005022:Ethyldimethylaminopropyl Carbodiimide