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THE INVOLVEMENT OF 1O 2 IN THE INACTIVATION OF MIXED FUNCTION OXIDASE AND PEROXIDATION OF MEMBRANE LIPIDS DURING THE PHOTOSENSITIZED OXIDATION OF LIVER MICROSOMES
Author(s) -
Rahimtula Anver D.,
Hawco Fred J.,
O'Brien Peter J.
Publication year - 1978
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1978.tb07023.x
Subject(s) - lipid peroxidation , microsome , chemistry , biochemistry , oxidase test , cytochrome , microsoma , cytochrome p450 , cytochrome c oxidase , reductase , cytochrome p450 reductase , enzyme , membrane lipids , cytochrome c , membrane , coenzyme q – cytochrome c reductase , mitochondrion
— Dye sensitized photooxidation of rat liver microsomes results in inactivation of mixed function oxidase and peroxidation of the membrane lipids. Both the flavoenzyme NADPH: cytochrome P450 reductase and cytochrome P450 components of the mixed function oxidase were inactivated. Singlet oxygen was responsible for these effects as the inactivation was markedly enhanced if the microsomes were in D 2 O buffer during the irradiation. Singlet oxygen quenchers or traps also protected the microsomes against enzyme inactivation and lipid peroxidation. Antioxidants, whilst preventing the lipid peroxidation, did not protect cytochrome P450 from inactivation which suggests that lipid peroxidation was not responsible for cytochrome P450 inactivation.