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Cooperative binding of oxygen to hemoglobin: Analysis of accurate equilibrium binding data
Author(s) -
Deal Walter J.
Publication year - 1973
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1973.360120912
Subject(s) - cooperativity , chemistry , allosteric regulation , hemoglobin , diphosphoglycerate , cooperative binding , oxygenation , equilibrium constant , oxygen , thermodynamics , computational chemistry , binding site , biochemistry , organic chemistry , receptor , physics , ecology , biology
Accurate equilibrium binding data for the oxygenation of hemoglobin are used (a) to show that various models for cooperativity are inconsistent with the best available experimental data, (b) to determine the equilibrium constants for binding of 2,3‐diphosphoglycerate to hemoglobin molecules in intermediate stages of oxygenation, and (c) to deduce a mechanism for allosteric effects in hemoglobin which is consistent with the best available experimental data. The total free energy of cooperativity is defined and discussed.