Reports

Conformational Equilibria in Spin-Labeled Hemoglobin

Science  19 Mar 1971:
Vol. 171, Issue 3976, pp. 1147-1149
DOI: 10.1126/science.171.3976.1147

Abstract

A component characteristic of deoxyhemoglobin appears in the paramagnetic resonance spectrum of spin-labeled oxyhemoglobin, and vice versa, under conditions of pH and ionic strength consistent with the interpretation that the spectrum is sensitive to the conformational equilibrium of the carboxy-terminal histidines. The oxygenation-induced change in the resonance spectrum is discussed in terms of shifts in this equilibrium.

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