Wallace C J
Biochem J. 1984 Feb 1;217(3):601-4. doi: 10.1042/bj2170601.
Acetimidylated horse cytochrome c and related derivatives exhibit more or less marked changes, both upscale and downscale, in apparent pK of the alkaline transition. This transition occurs when the normal methionine-80 residue is replaced at the sixth haem co-ordination position by another strong-field ligand. Analysis of the relationship between structural change and pK shift in these derivatives supports the view that the replacement ligand is a lysine residue, probably 72 or 79, and contradicts an alternative hypothesis. The results add further detail to a comprehensive view of the mechanism of this isomerization.
乙酰亚胺化马细胞色素c及相关衍生物在碱性转变的表观pK值上或多或少呈现出明显的变化,既有升高也有降低。当正常的甲硫氨酸-80残基在第六个血红素配位位置被另一个强场配体取代时,就会发生这种转变。对这些衍生物中结构变化与pK位移之间关系的分析支持了这样一种观点,即取代配体是一个赖氨酸残基,可能是72或79,这与另一种假设相矛盾。这些结果为这种异构化机制的全面观点增添了更多细节。