Abstract
The oxygenation of haemoglobin is accompanied by structural changes in the subunits triggered by shifts of the iron atoms relative to the porphyrin and, in the β-subunits, also by the steric effect of oxygen itself. The oxygen-free form is constrained by salt-bridges which are broken by the energy of haem–haem interaction with the release of H+. 2,3-Diphosphoglycerate may add to the constraints by being stereochemically complementary to a site between the β-chains ; this complementarity is lost on oxygenation.
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PERUTZ, M. Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery. Nature 228, 726–734 (1970). https://doi.org/10.1038/228726a0
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DOI: https://doi.org/10.1038/228726a0
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