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  • Title: Effect of superoxide dismutase on hydroxylase activity and hydrogen peroxide formation in anthranilamide hydroxylation by a rat liver microsomal monooxygenase system.
    Author: Ohta Y, Ishiguro I, Naito J, Shinohara R.
    Journal: Biochem Int; 1984 May; 8(5):617-27. PubMed ID: 6477624.
    Abstract:
    Anthranilamide was slightly hydroxylated by a reconstituted rat liver microsomal monooxygenase system with NADPH, but a large amount of hydrogen peroxide was formed with a consumption of NADPH during the reaction. Superoxide dismutase stimulated the hydroxylation by depressing the hydrogen peroxide formation, in that there was a reverse correlation between the two effects due to the dismutase. In addition, a trace of 3-hydroxyanthranilamide, one of the products, not only stimulated NADPH-dependent hydrogen peroxide formation via NADPH-cytochrome c (P-450) reductase, but also inhibited the reduction of cytochrome P-450 by NADPH in the reconstituted system. These effects of 3-hydroxyanthranilamide were also diminished by superoxide dismutase.
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