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. 1972 Feb;69(2):335–339. doi: 10.1073/pnas.69.2.335

Mechanism of Cooperative Oxygen Binding to Hemoglobin

Ronald T Ogata 1, Harden M McConnell 1
PMCID: PMC426452  PMID: 4333976

Abstract

Evidence is presented that a generalized concerted transition model provides a quantitative understanding of (a) the molecular species that are present in solutions of partially liganded hemoglobin and (b) the macromolecular mechanism of cooperativity. Model parameters for hemoglobin A and for hemoglobin Chesapeake were determined from studies of the binding of spin-label triphosphates to ligand-free and partially liganded hemoglobin solutions, and to the hybrids α2+CNβ2 and α2β2+CN. This model is the same as that proposed originally by Monod, Wyman, and Changeux [J. Mol. Biol. (1965) 12, 88] for hemoglobin, except that the α-subunits are treated as nonequivalent to the β-subunits.

Keywords: spin-labeled triphosphate, concerted transition model, hemoglobin Chesapeake

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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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