Study of nonequilibrium states of cyanide complexes of hemoglobin and myoglobin by a low-temperature inhibition method

Cyanide-ferrihemoglobin (myoglobin) interaction was studied by freeze-quenching technique and low-temperature ESR at various pH values. New ESR signals of these low-spin cyanide-protein complexes were recorded. These signals were interpreted as indication of the appearance of conformationally non-equilibrium states of these complexes. The relaxation to the equilibrium states of corresponding proteins takes about hundred milliseconds.