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Related Experiment Videos

Vanadate-stimulated NADH oxidation in microsomes.

M Rau, M S Patole, S Vijaya

    Molecular and Cellular Biochemistry
    |June 1, 1987
    PubMed
    Summary

    Vanadate stimulates NADH oxidation in rat liver microsomes, producing NAD+ and H2O2. This reaction, dependent on polymeric vanadate and low pH, is inhibited by various agents and linked to membrane electron transport.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Enzymology

    Background:

    • Rat liver microsomes catalyze NADH oxidation.
    • Vanadate is known to interact with biological systems.

    Purpose of the Study:

    • To investigate the effect of vanadate on NADH oxidation in rat liver microsomes.
    • To elucidate the mechanism and active species of vanadate in this reaction.

    Main Methods:

    • Spectrophotometric measurement of NADH disappearance at 340 nm.
    • Oxygen uptake measurements.
    • Inhibition studies with various chemical agents and enzymes.

    Main Results:

    • Vanadate addition stimulated NADH oxidation, yielding NAD+ and H2O2.
    • Polymeric vanadate was the active species, with optimal activity at low pH.
    • The reaction was inhibited by cyanide, EDTA, antioxidants, and metalloenzymes.
    • Mitochondrial outer membranes showed similar activity, but intact mitochondria inhibited microsomal activity.
    • Oxygen uptake and NADH disappearance were delinked, with vanadate acting as an electron acceptor.

    Conclusions:

    • Vanadate acts as an electron acceptor in NADH oxidation by microsomes.
    • A mechanism involving NAD radical and phosphovanadate is proposed.
    • Microsomes possess unique capabilities in reducing vanadate compared to other membranes.

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