Reduction of frozen water-glycerol solutions of methemoglobin by thermolysed electrons at 77 degrees K has been studied by Mossbauer spectroscopy. The formation of nonequilibrium hemoglobin states with two slightly different low-spin ferroforms was observed. The latter is explained by the presence of two ferroforms in initial methemoglobin. There was observed relaxation of the conformation - nonequilibrium states up to equilibrium hemoglobin with high-spin Fe(II) at the sample disfreezing.
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