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.
Archakov A.I., Zgoda V.G., Karuzina I.I. (1998) Oxidative modification of cytochrome P450 and other macromolecules during turnover. Voprosy Meditsinskoi Khimii, 44(1), 3-27.
Archakov A.I. et al. Oxidative modification of cytochrome P450 and other macromolecules during turnover // Voprosy Meditsinskoi Khimii. - 1998. - V. 44. -N 1. - P. 3-27.
Archakov A.I. et al., "Oxidative modification of cytochrome P450 and other macromolecules during turnover." Voprosy Meditsinskoi Khimii 44.1 (1998): 3-27.
Archakov, A. I., Zgoda, V. G., Karuzina, I. I. (1998). Oxidative modification of cytochrome P450 and other macromolecules during turnover. Voprosy Meditsinskoi Khimii, 44(1), 3-27.
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