[用穆斯堡尔谱学研究非平衡血红蛋白状态的弛豫]
[Study of the relaxation of nonequilibrium hemoglobin states by Mössbauer spectroscopy].
作者信息
Prusakov V E, Stukan R A, Davydov R M
出版信息
Biofizika. 1984 May-Jun;29(3):359-64.
PMID:6466715
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.
摘要
通过穆斯堡尔光谱研究了在低温（T = 77K）下热解电子还原其衍生物（高铁血红蛋白和氧合血红蛋白）形成的非平衡血红蛋白状态。观察到样品加热时非平衡状态的弛豫。指出了弛豫温度与根据穆斯堡尔数据确定的蛋白质动态结构变化之间的相关性。
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