高铁血红蛋白溶液中蛋白质和水质子的核磁共振弛豫
NMR relaxation of protein and water protons in methemoglobin solutions.
作者信息
Eisenstadt M
出版信息
Biophys J. 1981 Mar;33(3):469-74. doi: 10.1016/S0006-3495(81)84907-7.
Hemoglobin (Hb) proton spins rapidly equilibrate among themselves after an initial excitation, and relax toward thermal equilibrium as a unit. In the diamagnetic form, spin diffusion to nearby methyl relaxation sinks can account for this. For metHb, four strong heme relaxation centers dominate, and spin diffusion must occur over long distances. A sizeable difference in protein T1 is found between H2O and D2O solutions, much more than for diamagnetic Hb, consistent with internal H2O acting as a spin carrier to the heme.
血红蛋白（Hb）质子自旋在初始激发后会迅速在自身之间达到平衡，并作为一个整体弛豫至热平衡状态。在抗磁性形式中，自旋扩散到附近的甲基弛豫阱可以解释这一现象。对于高铁血红蛋白（metHb），四个强血红素弛豫中心起主导作用，自旋扩散必须在长距离上发生。在H2O和D2O溶液之间发现蛋白质T1存在相当大的差异，比抗磁性血红蛋白大得多，这与内部H2O作为血红素的自旋载体相一致。
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