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Related Experiment Videos

Interaction between low-affinity cupric ion and human methemoglobin.

W E Antholine, R Basosi, J S Hyde

    Journal of Inorganic Biochemistry
    |June 1, 1984
    PubMed
    Summary
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    Copper binds to human hemoglobin's beta chains, potentially oxidizing heme. This study located a low-affinity copper binding site near heme iron, suggesting proximal histidine involvement in heme oxidation and copper reduction.

    Area of Science:

    • Biochemistry
    • Protein Chemistry
    • Metalloproteins

    Background:

    • Human hemoglobin possesses high- and low-affinity cupric ion binding sites on its beta chains.
    • Copper bound to the low-affinity site is linked to selective oxidation of beta hemes.

    Purpose of the Study:

    • To pinpoint the location of the low-affinity cupric ion binding site in human hemoglobin.
    • To investigate the role of this binding site and proximal histidine in heme oxidation and copper reduction.

    Main Methods:

    • Spectroscopic analysis to locate the copper binding site.
    • Biochemical assays to assess heme oxidation and copper reduction.

    Main Results:

    • A low-affinity cupric ion binding site was identified within 10 Å of the heme iron in human hemoglobin.

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  • Evidence suggests proximal histidine involvement in copper binding at this site.

    • Conclusions:

    • The proximal histidine residue likely mediates copper binding, facilitating heme iron oxidation and cupric ion reduction.
    • This interaction offers new insights into hemoglobin's redox chemistry and copper's role.