固氮酶铁蛋白的电子顺磁共振谱模拟。对第二个顺磁中心存在的预测。
Simulation of the electron-paramagnetic-resonance spectrum of the iron-protein of nitrogenase. A prediction of the existence of a second paramagnetic centre.
作者信息
Lowe D J
出版信息
Biochem J. 1978 Dec 1;175(3):955-7. doi: 10.1042/bj1750955.
Abstract
The e.p.r. spectra of the Fe-proteins of nitrogenase from all sources studied have unusual features in that they have very anisotropic linewidths and low integrated intensities. These characteristics can be explained by assuming that one of the two electrons accepted by these proteins is located at a rapidly relaxing paramagnetic centre that is unobservable by e.p.r., but causes anisotropic broadening of the e.p.r. signal of the other electron. Complex-formation between Fe-proteins and MgATP is described in terms of a 50-60 degrees rotation of the e.p.r.-observable centre.
摘要
对所有已研究来源的固氮酶铁蛋白进行电子顺磁共振（EPR）光谱分析，发现其具有不同寻常的特征，即线宽极具各向异性且积分强度较低。这些特征可以通过以下假设来解释：这些蛋白质所接受的两个电子中的一个位于一个快速弛豫的顺磁中心，该中心无法通过电子顺磁共振观察到，但会导致另一个电子的电子顺磁共振信号出现各向异性展宽。铁蛋白与MgATP之间的复合物形成是根据电子顺磁共振可观察中心旋转50 - 60度来描述的。
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