Rein H, Ristau O, Ruckpaul K
Biochim Biophys Acta. 1975 Jun 26;393(2):373-8. doi: 10.1016/0005-2795(75)90064-1.
By means of electron spin resonance and magneto-optical rotation, specific low spin complexes in acidic methemoglobin are obtained. The formation of these complexes is explained by a specific stereochemical arrangement of the distal histidine in the absence of allosteric effectors inducing the formation of a low spin ligand at room temperature. At low temperature, however, the distal histidine is directly bound to the heme iron. As the formation of the low spin complexes depends on allosteric effectors it is suggested that via the distal histidine the affinity of heme iron ligands is modified.
通过电子自旋共振和磁光旋转，在酸性高铁血红蛋白中获得了特定的低自旋复合物。这些复合物的形成是由远端组氨酸在室温下不存在诱导低自旋配体形成的变构效应物时的特定立体化学排列来解释的。然而，在低温下，远端组氨酸直接与血红素铁结合。由于低自旋复合物的形成取决于变构效应物，因此表明通过远端组氨酸，血红素铁配体的亲和力发生了改变。
