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Cofactor Binding and Oxygen Equilibria in Haemoglobin

Nature New Biology volume 234, pages 174–176 (1971)Cite this article

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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Authors and Affiliations

  1. Department of Biochemistry, College of Physicians and Surgeons, Columbia University, New York, New York

    RUTH E. BENESCH, REINHOLD BENESCH & ROBERT RENTHAL

  2. MRC Biophysics Unit, King's College, 29 Drury Lane, London, WC2

    WALTER B. GRATZER

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  1. RUTH E. BENESCH
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BENESCH, R., BENESCH, R., RENTHAL, R. et al. Cofactor Binding and Oxygen Equilibria in Haemoglobin. Nature New Biology 234, 174–176 (1971). https://doi.org/10.1038/newbio234174a0

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