The EPR spectra of nitrosyl hemoglobin and myoglobin in different cond
itions (native, denatured and lyophilized), as well as of hematin-NO w
ere obtained in the temperature range of 80-280 K. There is a substant
ial and reversible decrease of the areas of the EPR spectra of all the
hemoglobin samples above 150 K. The interpretation of the results imp
lies the existence of two conformational states in thermal equilibrium
, only one of which is EPR detectable. Thermodynamical parameters are
determined for the hexa- and penta-coordinated cases.