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Analysis of the effects of chloride and 2,3‐diphosphoglycerate on the cooperative binding of oxygen to hemoglobin
Author(s) -
Deal Walter J.
Publication year - 1975
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.1975.360140615
Subject(s) - diphosphoglycerate , chemistry , cooperativity , hemoglobin , chloride , cooperative binding , oxygenation , ion , oxygen , inorganic chemistry , biophysics , binding site , biochemistry , organic chemistry , medicine , biology
Analysis of experimental equilibrium constants for the oxygenation of hemoglobin leads to a plausible mechanism for the effect of pH and of chloride ions on cooperativity in hemoglobin. According to this mechanism, the structural changes responsible for cooperativity in chloride‐ and 2,3‐diphosphoglycerate‐free hemoglobin are affected only slightly by changes in pH, and the effect of chloride can be accounted for by sequential binding and release of chloride ions during oxygenation.