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The function of catalase-bound NADPH.

H N Kirkman, S Galiano, G F Gaetani

    The Journal of Biological Chemistry
    |January 15, 1987
    PubMed
    Summary

    Catalase enzyme remains active during hydrogen peroxide exposure due to bound NADPH. This cofactor prevents and reverses inactive compound II formation, linking catalase and glutathione reductase pathways via NADPH dependency.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Cellular Biology

    Background:

    • Catalase (H2O2:H2O2 oxidoreductase, EC 1.11.1.6) is a historically significant enzyme.
    • The mechanism of catalase's sustained activity in the presence of its substrate, hydrogen peroxide, has been poorly understood.
    • Recent findings indicated catalase contains tightly bound NADPH.

    Purpose of the Study:

    • To investigate the role of bound NADPH in maintaining catalase activity.
    • To elucidate the protective mechanism of NADPH against hydrogen peroxide-induced inactivation.
    • To explore the implications of NADPH's role for cellular hydrogen peroxide metabolism.

    Main Methods:

    • Studied bovine and human catalase.
    • Investigated the effect of NADPH on catalase activity and compound II formation.
    • Assessed NADPH's protective effects at varying concentrations, including sub-micromolar levels.

    Main Results:

    • NADPH was confirmed to be tightly bound to catalase.
    • NADPH was shown to both prevent and reverse the formation of compound II, an inactive catalase intermediate.
    • The protective effect of NADPH was observed at concentrations below 0.1 microM, suggesting in vivo relevance.

    Conclusions:

    • Bound NADPH plays a crucial role in protecting catalase from self-inactivation by hydrogen peroxide.
    • This finding unifies the understanding of hydrogen peroxide disposal pathways, highlighting the central role of NADPH in both catalase and the glutathione reductase/peroxidase system.

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