Analysis of experimental equilibrium constants for the oxygenation of hemoglobin leads to a plausible mechanism for the effect of pH and of chloride ions on cooperativity in hemoglobin. According to this mechanism, the structural changes responsible for cooperativity in chloride‐ and 2,3‐diphosphoglycerate‐free hemoglobin are affected only slightly by changes in pH, and the effect of chloride can be accounted for by sequential binding and release of chloride ions during oxygenation.
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Walter J. Deal (1975) studied this question.
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