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High-affinity iron binding by xanthine oxidase.

G F Vile, C C Winterbourn

    Journal of Free Radicals in Biology & Medicine
    |January 1, 1986
    PubMed
    Summary

    Xanthine oxidase binds iron with high affinity, suggesting it may compete for iron within cells. This iron binding is significant for its role in Fenton reactions.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Metal-protein interactions

    Background:

    • Xanthine oxidase is a crucial enzyme involved in purine metabolism.
    • Understanding metal ion interactions with enzymes is vital for cellular processes.
    • Iron's role in biological systems, including potential catalytic activity, is of significant interest.

    Purpose of the Study:

    • To investigate the competitive binding of iron (59FeCl3) to xanthine oxidase in the presence of citrate or ATP.
    • To determine the affinity and stoichiometry of iron binding to xanthine oxidase.
    • To assess the implications of iron binding for xanthine oxidase function and intracellular iron competition.

    Main Methods:

    • Equilibrium dialysis was employed to study the binding of 59FeCl3 to xanthine oxidase.
    • Competitive binding assays were performed using citrate and ATP as chelators.
    • Iron binding affinity and site number were quantified.

    Main Results:

    • Xanthine oxidase exhibits high-affinity iron binding, with one high-affinity site per monomer.
    • The affinity constant for iron binding was determined to be 5 x 10^12 M^-1.
    • Iron binding to xanthine oxidase was observed even in the presence of chelators like citrate and ATP.

    Conclusions:

    • Xanthine oxidase likely binds iron in many in vitro experimental settings.
    • The enzyme has the potential to compete for intracellular chelatable iron.
    • The bound iron may play a role as a catalyst in Fenton reactions, with implications for oxidative stress.

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