混合态血红蛋白中铁的自旋弛豫
Spin relaxation of iron in mixed state hemoproteins.
作者信息
Wajnberg E, Kalinowski H J, Bemski G, Helman J S
出版信息
Biophys J. 1986 Jun;49(6):1195-8. doi: 10.1016/S0006-3495(86)83747-X.
Abstract
In hemoproteins the relaxation mechanism of iron is Orbach for high spin (HS) and Raman for low spin (LS). We found that in met-hemoglobin and met-myoglobin, under conditions in which the two spin states coexist, both the HS and the LS states relax to the lattice through Orbach-like processes. Alos, very short (approximately 1 ns) and temperature independent transverse relaxation times T2 were estimated. This may result from the unusual electronic structure of mixed states hemoproteins that allows thermal equilibrium and interconversion of the spin states.
摘要
在血红素蛋白中，铁的弛豫机制对于高自旋（HS）态是奥尔巴赫过程，对于低自旋（LS）态是拉曼过程。我们发现，在高铁血红蛋白和高铁肌红蛋白中，在两种自旋态共存的条件下，HS态和LS态都通过类似奥尔巴赫的过程弛豫到晶格。此外，还估计出了非常短（约1纳秒）且与温度无关的横向弛豫时间T2。这可能是由于混合态血红素蛋白异常的电子结构，使得自旋态能够达到热平衡并相互转换。
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