Coboglobins: heterotropic linkage and the existence of a quaternary structure change upon oxygenation of cobaltohemoglobin.

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.