Conformational Equilibria in Spin-Labeled Hemoglobin
Walter J. Deal 1,
Susan G. Mohlman 1, and
Marcia L. Sprang 1
1 Department of Chemistry, University of California, Riverside 92502
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.