PARTICIPATION OF SUPEROXIDE, HYDROGEN-PEROXIDE AND HYDROXYL RADICALS IN NADPH-CYTOCHROME P-450 REDUCTASE-CATALYZED PEROXIDATION OF METHYL LINOLENATE

  • 1 January 1979
    • journal article
    • research article
    • Vol. 572  (1) , 77-82
Abstract
NADPH-cytochrome P-450 reductase[from rat liver]-catalyzed peroxidation of methyl linolenate is inhibited by superoxide dismutase, catalase, ethanol, and mannitol and is potentiated by H2O2. H2O2 is generated in the incubation mixture in the presence of NADPH and NADPH-cytochrome P-450 reductase. If the system contains Fe-EDTA complex, H2O2 is not formed. In the presence of the enzyme and Fe-EDTA complex, added H2O2 is is consumed. In the presence of Fe-EDTA complex, NADPH-cytochrome P-450 reductase generates .**GRAPHIC**. at a slow rate. H2O2 produced from .**GRAPHIC**. is probably decomposed to form OH.cntdot. by the action of Fe-EDTA complex in the lipid peroxidation system, with OH.cntdot. as a trigger of lipid peroxidation.

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