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Concerning the metalloenzyme ascorbate oxidase

K G Krul, C R Dawson

    Bioinorganic Chemistry
    |January 1, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Apoascorbate oxidase, lacking copper, exhibits reduced structural stability and undergoes dissociation unlike native ascorbate oxidase. This study details the conformational and stability differences between apo- and holo-ascorbate oxidase.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Protein Chemistry

    Background:

    • Ascorbate oxidase is a copper-containing enzyme crucial for plant defense and cell wall metabolism.
    • Understanding the structural and functional roles of copper in ascorbate oxidase is essential for elucidating its catalytic mechanisms.
    • Apoascorbate oxidase, the copper-depleted form, serves as a critical model for investigating copper's contribution to enzyme stability and activity.

    Purpose of the Study:

    • To characterize the structural and conformational properties of apoascorbate oxidase.
    • To compare the stability and quaternary structure of apoascorbate oxidase with native and holoascorbate oxidase.
    • To investigate the aging process of apoascorbate oxidase and its impact on protein structure.

    Main Methods:

    Related Experiment Videos

  • Gel electrophoresis (polyacrylamide gel electrophoresis, SDS-PAGE)
  • Ultracentrifugation (sedimentation velocity)
  • Isoelectric focusing

    • Main Results:

    • Apoascorbate oxidase has a molecular weight of 137,000 +/- 3,000, similar quaternary conformation to native ascorbate oxidase, but lacks conformational stability.
    • Copper removal and disulfide bond reduction yield a less stable apoenzyme.
    • Aging apoascorbate oxidase leads to tyrosine residue loss and subunit dissociation, unlike stable native/holoenzymes.
    • Holoascorbate oxidase has a molecular weight of 285,000 and an s020,w of 9.79.
    • Holoascorbate oxidase exhibits 23% lower electrophoretic mobility than native or apoenzyme.
    • Electrophoresis and isoelectric focusing of holoenzyme show greater similarity to apoascorbate oxidase than native enzyme.

    Conclusions:

    • Apoascorbate oxidase is conformationally less stable than native and holoascorbate oxidase due to copper removal and disulfide bond reduction.
    • The aging process of apoascorbate oxidase involves structural degradation, including subunit dissociation.
    • Copper is critical for maintaining the structural integrity and stability of ascorbate oxidase.