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Related Experiment Videos

Iron and aconitase activity.

O Gawron, A Waheed, A J Glaid

    The Biochemical Journal
    |June 1, 1974
    PubMed
    Summary

    Active aconitase requires one iron (Fe2+) atom per molecule for function. This essential iron is lost to chelators, inactivating the enzyme, with ascorbate accelerating iron loss and citrate slowing it.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Metalloprotein characterization

    Background:

    • Aconitase is a key enzyme in the citric acid cycle.
    • The role of iron in aconitase activity requires further elucidation.

    Purpose of the Study:

    • To investigate the stoichiometry of iron incorporation into active aconitase.
    • To determine the impact of iron availability and chelators on aconitase activity.
    • To characterize the iron-binding site of aconitase.

    Main Methods:

    • Enzyme activity assays with varying iron concentrations.
    • Iron chelation studies using ferrozine.
    • Investigating the effects of ascorbate and citrate on iron transfer.
    • Urea-induced iron transfer from inactive aconitase.

    Main Results:

    • Aconitase incorporates one specific iron (Fe2+) atom per molecule upon activation.
    • Loss of this iron to ferrozine abolishes enzyme activity.
    • Ascorbate enhances Fe2+ transfer, while citrate inhibits it.
    • Inactive aconitase contains two iron atoms, and Fe2+ can be transferred under specific conditions.

    Conclusions:

    • Active aconitase possesses a single essential Fe2+ binding site.
    • Enzyme activity is directly correlated with the presence of this single iron atom.
    • Iron homeostasis is critical for aconitase function.

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