Mechanism of Cooperative Oxygen Binding to Hemoglobin
- 1 February 1972
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 69 (2), 335-339
- https://doi.org/10.1073/pnas.69.2.335
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 alpha(2) (+CN)beta(2) and alpha(2)beta(2) (+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 alpha-subunits are treated as nonequivalent to the beta-subunits.Keywords
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