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Hydrogen peroxide‐supported activities of semisynthetic flavocytochrome 2B4
Author(s) -
Shumyantseva Victoria V.,
Avdeenko Yuliya L.,
Moskvitina Tatyana L.,
Bulko Tatyana V.,
Archakov Alexander I.
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800202542
Subject(s) - chemistry , hydrogen peroxide , aniline , hydroxylation , peroxide , catalysis , demethylation , covalent bond , chemiluminescence , sodium cyanide , enzyme kinetics , active site , medicinal chemistry , enzyme , organic chemistry , cyanide , biochemistry , gene expression , dna methylation , gene
Semisynthetic flavocytochromes, obtained by covalent binding of riboflavin with cytochromes P450 2B4, were able to catalyze the H202‐mediated reactions of aniline p‐hydroxylation, aminopyrine N‐demethylation and p‐nitroanizole O‐dealkylation. The rates of the flavocytochrome‐catalyzed, H202‐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, Km) 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.