Wallace C J
Biochem J. 1984 Feb 1;217(3):595-9. doi: 10.1042/bj2170595.
The biological consequences of acetimidylation of all 19 epsilon-amino groups of horse cytochrome c are a slight decrease in both the redox potential of the protein and its ability to stimulate oxygen uptake in the cytochrome c-depleted-mitochondria assay. Examination of a number of specific partially acetimidylated analogues and acetimidylated cytochromes c of other species has shown that the changes in biological properties, which are associated with a slight structural change as monitored by n.m.r. spectroscopy [Boswell, Moore, Williams, Harris, Wallace, Bocieck & Welti (1983) Biochem. J. 213, 679-686], appear to stem from modification of residues in a restricted region of the sequence. The failure of the redox potential of Saccharomyces cerevisae cytochrome c to be affected by acetimidylation suggests that it is lysine-53, absent from that species, that is the sensitive residue.
马细胞色素c的全部19个ε-氨基被乙酰亚胺化后的生物学后果是,该蛋白质的氧化还原电位及其在细胞色素c缺失的线粒体分析中刺激氧气摄取的能力均略有下降。对多种特定的部分乙酰亚胺化类似物以及其他物种的乙酰亚胺化细胞色素c的研究表明,与通过核磁共振光谱监测到的轻微结构变化相关的生物学特性变化[Boswell、Moore、Williams、Harris、Wallace、Bocieck和Welti(1983年)《生物化学杂志》213卷,679 - 686页],似乎源于序列中一个受限区域内残基的修饰。酿酒酵母细胞色素c的氧化还原电位不受乙酰亚胺化影响,这表明该物种中不存在的赖氨酸-53是敏感残基。