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  • Title: Participation of superoxide, hydrogen peroxide and hydroxyl radicals in NADPH-cytochrome P-450 reductase-catalyzed peroxidation of methyl linolenate.
    Author: Kameda K, Ono T, Imai Y.
    Journal: Biochim Biophys Acta; 1979 Jan 29; 572(1):77-82. PubMed ID: 32915.
    Abstract:
    1. NADPH-cytochrome P-450 reductase-catalyzed peroxidation of methyl linolenate is inhibited by superoxide dismutase, catalase, ethanol, and mannitol, and is potentiated by H2O2. 2. H2O2 is shown to be 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 consumed. 3. In the presence of Fe-EDTA complex, NADPH-cytochrome P-450 reductase is shown to generate O-2 at a slow rate. These results suggest that H2O2 produced from O-2 is decomposed to form OH . by the action of Fe-EDTA complex in the lipid peroxidation system, and that OH . is a trigger of lipid peroxidation.
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