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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1973 Jan;70(1):1–4. doi: 10.1073/pnas.70.1.1

The Contribution of the α and β Chains to the Kinetics of Oxygen Binding to and Dissociation from Hemoglobin

Quentin H Gibson 1
PMCID: PMC433169  PMID: 4509652

Abstract

A new type of experiment in which hemoglobin is exposed briefly to oxygen has shown that the half-time of dissociation of oxygen from some partly oxygenated intermediates is about 1 msec at 20° and 10 msec at 2°. The rapid dissociation occurs selectively from one type of chain, provisionally identified as the β-chain. Chains that show the rapid rate of dissociation of oxygen also bind rapidly. It follows that the kinetic equivalent of the Adair equation and the Monod-Wyman-Changeux model are quite unsuited to represent the kinetics of the oxygen-hemoglobin reaction. The reaction of oxygen with hemoglobin closely resembles that of the alkyl isocyanides and differs radically from that of carbon monoxide.

Keywords: heme proteins, ligand binding, protein chemistry

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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