Cofactor Binding and Oxygen Equilibria in Haemoglobin |
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Authors: | RUTH E. BENESCH REINHOLD BENESCH ROBERT RENTHAL WALTER B. GRATZER |
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Affiliation: | 1.Department of Biochemistry,Columbia University, College of Physicians and Surgeons,New York;2.MRC Biophysics Unit,King's College,London |
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Abstract: | THE oxygen affinity of haemoglobin is profoundly affected by the presence of low concentrations of organic phosphates, in particular 2,3-diphosphoglycerate (DPG)1–5. This phenomenon, which has now been widely recognized as a physiologically vital control mechanism6–10, can be explained qualitatively by our observations2 that deoxyhaemoglobin has a single strong binding site for the cofactor, which in consequence stabilizes it in relation to the oxygenated state. The binding site is associated with the β chains11 and it has been identified as the cavity at the conjunction of the N-termini of these chains5,12–18, lying therefore on the dyad axis of the tetramer. |
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