A comparative study of pH/activity profiles for the anaerobic H2O2 and alkyl hydroperoxide supported N demethylation of N methylaniline catalyzed by alkaline haematin and microsomal cytochrome P-450.
A comparative study of the effect of pH on haemin-mediated H2O2 and alkyl hydroperoxide-supported N-demethylation of N-methylaniline and the corresponding cytochrome P-450 mediated process has been carried out. This extends previous studies and provides quantitative evidence that the same active oxygen species are involved in both the enzymic and metalloporphyrin mediated processes. Furthermore, this evidence clearly indicates that the environment at the point of catalysis in the enzyme active site differs considerably from that of the bulk solution.
Adams
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Department of Chemical Pathology, University of Cape Town Medical School, Republic of South Africa.
Adams
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D000693:Anaerobiosis; D000814:Aniline Compounds / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D001555:Benzene Derivatives / Q000494:pharmacology; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006427:Hemin / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008861:Microsomes / Q000201:enzymology*; D010545:Peroxides / Q000494:pharmacology; D020122:tert-Butylhydroperoxide
D000814:Aniline Compounds; D001555:Benzene Derivatives; D010545:Peroxides; D006427:Hemin; D003577:Cytochrome P-450 Enzyme System; D020122:tert-Butylhydroperoxide; D006861:Hydrogen Peroxide; C007164:cumene hydroperoxide; C021313:methylaniline