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Related Experiment Videos

Electrostatic effects in hemoglobin: electrostatic energy associated with allosteric transition and effector binding.

J B Matthew, S H Friend, F R Gurd

    Biochemistry
    |February 3, 1981
    PubMed
    Summary

    This study models hemoglobin stabilization, finding that 2,3-diphosphoglycerate and carbamino adducts compete for binding. This competition accurately predicts hemoglobin

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    Area of Science:

    • Biochemistry
    • Physiological Chemistry
    • Computational Biology

    Background:

    • Hemoglobin's oxygen-binding properties are modulated by various allosteric effectors.
    • Understanding the electrostatic stabilization of hemoglobin is crucial for explaining its functional behavior.
    • The Bohr effect and effector binding significantly influence hemoglobin's affinity for oxygen.

    Purpose of the Study:

    • To compute the pH dependence of electrostatic stabilization for deoxy- and liganded hemoglobin.
    • To investigate the binding behavior and contribution of 2,3-diphosphoglycerate (2,3-DPG) to hemoglobin stabilization and the alkaline Bohr effect.
    • To model the competitive interactions between 2,3-DPG, carbamino adducts, and other anions.

    Main Methods:

    • Computational modeling of electrostatic stabilization for hemoglobin.

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  • Calculation of effector binding contributions at various ionic strengths and pH values.
  • Formulation of a competitive binding model for 2,3-DPG, carbamino adducts, and anions.

    • Main Results:

    • Computed stabilization of deoxyhemoglobin by 2,3-DPG binding aligned with experimental data for human hemoglobins A0 and F.
    • The model accurately predicted the contribution of 2,3-DPG to the alkaline Bohr effect for both hemoglobins.
    • A competitive binding model explained the interplay between 2,3-DPG and Val-1 beta carbamino adducts, and simple anions.

    Conclusions:

    • The electrostatic stabilization of hemoglobin is pH-dependent and influenced by multiple allosteric effectors.
    • A competitive binding model successfully describes the interactions of 2,3-DPG, carbamino adducts, and anions with hemoglobin.
    • The model accurately predicts hemoglobin's functional behavior across physiological pH and effector concentrations.