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. 1972 Aug;69(8):2122–2124. doi: 10.1073/pnas.69.8.2122

Coboglobins: Heterotropic Linkage and the Existence of a Quaternary Structure Change Upon Oxygenation of Cobaltohemoglobin

G C Hsu 1, C A Spilburg 1, C Bull 1, B M Hoffman 1
PMCID: PMC426882  PMID: 4506082

Abstract

Cobaltohemoglobin prepared from horse hemoglobin retains the full heterotropic linkage properties of the normal iron hemoglobin, including both the Bohr and phosphate effects. From this result, and the known connection between heterotropic linkage properties and hemoglobin conformational change, it is concluded that cobaltohemoglobin undergoes a quaternary structure transition upon oxygenation. Thus, the stereochemical changes that occur upon oxygen binding to cobalt, as well as to iron, must be compatible with the mechanism triggering such a transition.

Keywords: Bohr effect; 2,3-diphosphoglycerate

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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