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The interaction of nitric oxide with ascorbate oxidase.

F X Leeuwen, R Wever, B F Gelder

    Biochimica Et Biophysica Acta
    |October 22, 1975
    PubMed
    Summary

    Nitric oxide interacts with ascorbate oxidase, causing reversible changes in copper centers. This interaction affects electron transfer and spectral properties without altering the enzyme's activity.

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    Area of Science:

    • Biochemistry
    • Bioinorganic Chemistry

    Background:

    • Ascorbate oxidase (L-ascorbate: oxygen oxidoreductase, EC 1.10.3.3) is a multi-copper enzyme.
    • Understanding its interaction with small molecules like nitric oxide (NO) is crucial for elucidating its catalytic mechanisms and potential regulatory roles.

    Purpose of the Study:

    • To investigate the reaction of nitric oxide with oxidized and reduced ascorbate oxidase.
    • To compare the effects of nitric oxide on ascorbate oxidase with those observed in ceruloplasmin.
    • To characterize the changes in copper centers upon nitric oxide interaction.

    Main Methods:

    • Optical absorption measurements.
    • Electron paramagnetic resonance (EPR) spectroscopy.
    • Anaerobic incubation techniques.

    Main Results:

    • Nitric oxide induces a decrease in absorbance at 610 nm in oxidized ascorbate oxidase, attributed to electron transfer to Type-1 copper.
    • Nitric oxide treatment leads to a decrease in EPR absorbance, with a predominant signal from Type-2 copper and vanishing of the Type-1 copper signal.
    • Quantitative analysis of EPR signals suggests the presence of one Type-2 and three Type-1 copper atoms per ascorbate oxidase molecule.
    • The observed spectral changes induced by nitric oxide are reversible, and the enzyme activity is restored upon NO removal.

    Conclusions:

    • Nitric oxide interacts with both Type-1 and Type-2 copper centers in ascorbate oxidase.
    • The interaction involves electron transfer and is reversible, with no lasting impact on enzymatic activity.
    • These findings provide insights into the redox properties and copper coordination environment of ascorbate oxidase.

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