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[Study of the relaxation of nonequilibrium hemoglobin states by Mössbauer spectroscopy]
Biofizika
|May 1, 1984
Abstract:
Nonequilibrium hemoglobin states formed at low-temperature (T = 77K) reduction of its derivatives (MetHb and HbO2) by thermolysed electrons have been studied by Mössbauer spectroscopy. Relaxation of nonequilibrium states at the samples heating was observed. Correlation between the relaxation temperatures and the changes of protein dynamic structure determined from Mössbauer data were stated.