[O-demethylation kinetics of anisole and p-chloroanisole by cumene hydroperoxide and cytochrome P-450 of liver microsomes].
The kinetics of anisole oxidation by microsomes and tertiary butylhydroperoxide have been studied in phosphate buffer (pH 7,4) at 37 degrees C. About 20% of the substrate are shown to undergo demetylation and about 80% were hydroxylated in the p-position. The kinetics of the oxidative o-demethylation of anisole and p-chloroanisole by cumene hydroperoxide and hepatic microsomes has been studied within the temperature range of 20--37 degrees C. The catalytic rate constants for o-demethylation of anisole and chloroanisole have been determined in a general form to equal 2,04.10(7) exp (--11400/RT) and 5,5.10(7) exp (--11800/RT) sec-1, respectively. The reactions of o-demethylation and hydroperoxide have been proved to be independent. The data obtained are indicative of the electrophilic nature of the hydroxylating agent in the system "microsomes-hydroperoxide".
D000818:Animals; D000840:Anisoles / Q000378:metabolism*; D001593:Benzyl Compounds / Q000494:pharmacology*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D003640:Dealkylation; D006900:Hydroxylation; D008862:Microsomes, Liver / Q000378:metabolism*; D010084:Oxidation-Reduction; D010545:Peroxides / Q000494:pharmacology*; D051381:Rats
D000840:Anisoles; D001593:Benzyl Compounds; D010545:Peroxides; D003577:Cytochrome P-450 Enzyme System
Kinetika O-demetilirovaniia anizola i p-khloranizola pri uchastii tsitokhroma P-450 mikrosom pecheni i gidroperekiseĭ.