[Study of the relaxation of nonequilibrium hemoglobin states by Mössbauer spectroscopy].
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.
D000818:Animals; D005720:Gamma Rays; D066298:In Vitro Techniques; D008706:Methemoglobin / Q000528:radiation effects; D051379:Mice; D010108:Oxyhemoglobins / Q000528:radiation effects; D011487:Protein Conformation / Q000528:radiation effects; D013057:Spectrum Analysis; D013696:Temperature
D010108:Oxyhemoglobins; D008706:Methemoglobin
Issledovanie relaksatsii neravnovesnykh sostoianiĭ gemoglobina metodom GR-spektroskopii.