McDermott P, May L, Orlando J
Biophys J. 1967 Sep;7(5):615-20. doi: 10.1016/S0006-3495(67)86610-4.
The Mössbauer spectra of horse heart ferri- and ferrocytochrome c were obtained at room temperature using lyophilized powders. The Mössbauer data indicate that the iron in both lyophilized samples is in a low-spin state. The high quadrupole splittings suggest that the iron atom is in an asymmetric ligand field. Upon reduction the asymmetry increases, suggesting a change in the bonding between the protein moieties and the iron atom.
使用冻干粉末在室温下获得了马心铁细胞色素c和亚铁细胞色素c的穆斯堡尔光谱。穆斯堡尔数据表明,两个冻干样品中的铁均处于低自旋态。高四极分裂表明铁原子处于不对称配体场中。还原后不对称性增加,表明蛋白质部分与铁原子之间的键合发生了变化。