title: [Oxidative modification of cytochrome P450 and other macromolecules during its turnover].
abstract: Possible mechanisms of cytochrome P4502B4 modification by H2O2 formed during catalytic turnover have been studied. Oxidative self-inactivation of cytochrome P4502B4 in monooxygenase system, reconstituted from highly purified membrane proteins: cytochrome P4502B4, NADDPH-cytochrome P450 reductase and cytochrome b5 in the presence of detergent Emulgen 913, involves the heme destruction and apoenzyme modification. The cytochrome P450 self-inactivation is accompanied by protein aggregation, oxidation of SH-groups and changes of the surface charge. H2O2 and non-specific radical reactions may be responsible for the intermolecular cross-linking. Oxidative modification of cytochrome P4502B4 may be initial stage of the protein decay in the cell.
authors.affiliation: Institute of Biomedical Chemistry, Moscow.
authors.forename: A I
authors.initials: AI
authors.lastname: Archakov
authors.forename: V G
authors.initials: VG
authors.lastname: Zgoda
authors.forename: I I
authors.initials: II
authors.lastname: Karuzina
mesh_terms: D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004789:Enzyme Activation; D006861:Hydrogen Peroxide / Q000378:metabolism; D010084:Oxidation-Reduction
chemical_list: D003577:Cytochrome P-450 Enzyme System; D006861:Hydrogen Peroxide
vernacular_title: Okislitel'naia modifikatsiia tsitokhroma P450 i drugikh makromolekul v protsesse ikh obnovleniia.