[Comparative inhibitory analysis of aniline hydroxylation by cytochrome P-450 in NADPH-, hydroperoxide cumyl- and H2O2-dependent systems].
The p-hydroxylation of aniline in the presence of liver microsomes and isolated cytochrome P-450 in NADPH-, H2O2- and cumyl hydroperoxide (CHP)-dependent systems was investigated. A comparative inhibitory analysis of these reactions was carried out. It was shown that the mechanism of the H2O2-dependent hydroxylation reactions is similar to that of the NADPH-dependent monooxygenase reactions and, consequently, this model system should be preferably used for the study of the mechanisms of aniline hydroxylation reactions instead of the CHP-dependent system. Since the kcat value for the H2O2-dependent system is much higher than that for the NADPH- or CHP-systems, it may be assumed that when H2O2 is used as a cosubstrate for this reaction, the true value of the degradation constant for the cytochrome P-450--O2(2-)--aniline peroxycomplex can be measured.
D000815:Aniline Hydroxylase / Q000037:antagonists & inhibitors*; D000818:Animals; D001189:Aryl Hydrocarbon Hydroxylases / Q000037:antagonists & inhibitors*; D001555:Benzene Derivatives / Q000494:pharmacology; D065607:Cytochrome P-450 Enzyme Inhibitors; D006861:Hydrogen Peroxide / Q000494:pharmacology; D006900:Hydroxylation; D007700:Kinetics; D008297:Male; D008862:Microsomes, Liver / Q000378:metabolism*; D009249:NADP / Q000494:pharmacology; D011485:Protein Binding; D011817:Rabbits
D001555:Benzene Derivatives; D065607:Cytochrome P-450 Enzyme Inhibitors; D009249:NADP; D006861:Hydrogen Peroxide; D000815:Aniline Hydroxylase; D001189:Aryl Hydrocarbon Hydroxylases; C007164:cumene hydroperoxide
Sravnitel'nyĭ ingibitornyĭ analiz gidroksilirovaniia anilina tsitokhromom P-450 v NADPH-, gidroperekis' kumila- i H202- zavisimykh sistemakh.