Asymmetric ligand binding by haemoglobin

Abstract

The asymmetry observed in the titration curve of haemoglobin with oxygen is possible only if the α-α and β-β subunit interactions change by different amounts on oxygenation. This necessary difference justifies the α2β2 structure on functional grounds and its magnitude shows that haemoglobin function results from reversible oxygen binding to the β subunit.

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Weber, G. Asymmetric ligand binding by haemoglobin. Nature 300, 603–607 (1982). https://doi.org/10.1038/300603a0

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