In the physiology of oxygen-hemoglobin binding, an important role is played by the influence of H⁺ and CO₂ on the affinity of hemoglobin for O₂. Here we extend the allosteric model of hemoglobin to include these effects. We assume purely allosteric modulation, i.e., that the modulatory effects of H⁺ and CO₂ on oxygen binding occur only because of their influence on the T ↔ R transition, in which all four subunits of the hemoglobin molecule participate simultaneously. We assume, moreover, that these modulatory influences occur only through the interaction of H⁺ and CO₂ with the amino group at the N-terminal of each of the four polypeptide chains of the hemoglobin molecule. We fit the model to experimental data and obtain reasonable agreement with the observed shifts in oxygen-hemoglobin binding that occur when the concentrations of H⁺ and CO₂ are changed.
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Huang et al. (2024) studied this question.
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