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Tadpole Xenopus laevis hemoglobin. Correlation between structure and functional properties.

M Brunori, S G Condò, A Bellelli

    Journal of Molecular Biology
    |January 20, 1985
    PubMed
    Summary

    Hemoglobin

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    Area of Science:

    • Biochemistry
    • Physiology
    • Molecular Biology

    Background:

    • The Root effect in hemoglobin influences oxygen binding.
    • The alkaline Bohr effect modulates hemoglobin's oxygen affinity.
    • Specific amino acid residues are implicated in these effects.

    Purpose of the Study:

    • To investigate the role of COOH-terminal His and Ser F9 in amphibian hemoglobin.
    • To test the Perutz & Brunori (1982) model for Root and alkaline Bohr effects.
    • To explain the absence of alkaline Bohr effect in some amphibians.

    Main Methods:

    • Kinetic analysis of carbon monoxide binding to Xenopus laevis hemoglobin.
    • Comparative analysis of hemoglobin function in different amphibian groups.

    Main Results:

    • Kinetic data support the proposed role of His and Ser F9 in the Root effect.
    • The findings provide a mechanistic explanation for the lack of alkaline Bohr effect in many aquatic Anura and Urodela.
    • Hemoglobin's COOH-terminal residues are critical for its functional properties.

    Conclusions:

    • The Perutz & Brunori model is supported by kinetic data from Xenopus laevis hemoglobin.
    • Specific beta-chain residues explain the Root effect and influence the alkaline Bohr effect.
    • This research clarifies hemoglobin adaptation in amphibians.

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