Abstract
The formation constants of the azide complexes of human methaemoglobins A and C have been measured as a function of pH and temperature. The hydrogen-ion uptake in these reactions has been measured as a function of pH and temperature. The customary interpretation of the pH-dependence of the affinity of a methaemoglobin for a ligand in terms of one or two “haem-linked” groups is shown to be invalid, and an alternative mechanism is proposed. The wider implications of this mechanism are discussed.
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