Divalent metals in the regulation
of hemoglobin affinity for oxygen
Bennun, A., Seidler, N. and De Bari, V.A.
It has previously been demonstrated that a model based on
intramolecular interac¬tions could satisfactorily predict
the effect of 2,3-diphosphoglycerate (2,3 DPG) on oxygen-hemoglobin
dissociation. Central to this model is the concept that in
proteins subject to allosteric interactions, the T state exhibits
hindering steric interaction of amino-acid side chains. In
this work, that concept is extended to include interactions
at the a1ß2 interface of the Hb molecule involving divalent
cations, as exemplified by Zn2+.
Annals of the New York Academy of Sciences, 463, (1986), 76-79