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Structure-specific model of hemoglobin cooperativity.

A W Lee, M Karplus

    Proceedings of the National Academy of Sciences of the United States of America
    |December 1, 1983
    PubMed
    Summary
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    This study presents a generalized statistical mechanical model for hemoglobin cooperativity, explaining thermodynamic and structural data. It reveals pH-independent cooperativity and specific salt bridge roles in oxygen binding.

    Area of Science:

    • Biophysics
    • Structural Biology
    • Biochemistry

    Background:

    • Hemoglobin cooperativity describes how oxygen binding to one subunit affects others.
    • Existing models like Monod-Wyman-Changeux and Perutz explain aspects of this phenomenon.
    • Understanding cooperativity is key to hemoglobin's oxygen transport function.

    Purpose of the Study:

    • To formulate a generalized statistical mechanical model for hemoglobin cooperativity.
    • To integrate thermodynamic, spectroscopic, and structural data.
    • To elucidate the roles of non-salt-bridge constraints and salt-bridge coupling in ligand binding.

    Main Methods:

    • Generalization of the Szabo-Karplus statistical mechanical model.
    • Fitting the model to available thermodynamic and spectroscopic data.

    Related Experiment Videos

  • Analysis of proton release data across a range of pH values.

    • Main Results:

    • The generalized model successfully fits experimental data and aligns with structural and energetic calculations.
    • A pH-independent component of hemoglobin cooperativity was identified.
    • Analysis of Adair constants suggests partial salt bridge linkage to ligation in the deoxy state and destabilization in the oxy state.

    Conclusions:

    • The developed model offers a comprehensive mechanism for hemoglobin cooperativity, extending previous proposals.
    • Non-salt-bridge interactions significantly influence ligand affinity.
    • Salt bridges play a dynamic role in mediating structural changes during oxygen binding.