Shumyantseva V V, Avdeenko Y L, Moskvitina T L, Bulko T V, Archakov A I
Institute of Biomedical Chemistry, Moscow, Russia.
Biochem Mol Biol Int. 1998 Jun;45(1):171-9. doi: 10.1080/15216549800202542.
Semisynthetic flavocytochromes, obtained by covalent binding of riboflavin with cytochromes P450 2B4, were able to catalyze the H2O2-mediated reactions of aniline p-hydroxylation, aminopyrine N-demethylation and p-nitroanizole' O-dealkylation. The rates of the flavocytochrome-catalyzed, H2O2-supported reactions far exceeded those of the appropriate NADH-dependent reactions and were comparable with the cytochrome P450 2B4-catalyzed, peroxide-mediated reaction rates. The kinetic parameters (kcat, K(m)) for the peroxide-dependent flavocytochrome P450 2B4 reactions were obtained. Sodium cyanide and SKF-525A, a specific P450 inhibitor, were both shown to inhibit these reactions. The generation of active oxygen species by flavocytochrome 2B4 was registered by chemiluminescence intensity.