脱水血红蛋白与脱水肌红蛋白中铁键的比较。
A comparison of the iron bonding in anhydrohemoglobin and anhydromyoglobin.
作者信息
Grant R W, Topol L E
出版信息
Biophys J. 1969 Dec;9(12):1446-50. doi: 10.1016/S0006-3495(69)86464-7.
Abstract
Mössbauer effect measurements show that the ferrous ions in dehydrated deoxymyoglobin are in the high spin state while those in dehydrated deoxyhemoglobin (AHb) are equally distributed between high and low spin states. It is concluded that the two spin states present in AHb are associated with the iron site difference of the alpha- and beta-chains.
摘要
穆斯堡尔效应测量结果表明，脱水脱氧肌红蛋白中的亚铁离子处于高自旋态，而脱水脱氧血红蛋白（AHb）中的亚铁离子则在高自旋态和低自旋态之间均匀分布。由此得出结论，AHb中存在的两种自旋态与α链和β链的铁位点差异有关。
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本文引用的文献
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Spin States of divalent iron in anhydrohemoglobin.脱辅基血红蛋白中二价铁的自旋态
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