还原时高铁细胞色素c的显著稳定化。

Dramatic stabilization of ferricytochrome c upon reduction.

作者信息

Hilgen-Willis S, Bowden E F, Pielak G J

机构信息

Department of Chemistry, University of North Carolina, Chapel Hill.

出版信息

J Inorg Biochem. 1993 Aug 15;51(3):649-53. doi: 10.1016/0162-0134(93)85036-8.

DOI:10.1016/0162-0134(93)85036-8

PMID:8409982

Abstract

By combining measurements of the free energy of denaturation of the C102T variant of Saccharomyces cerevisiae iso-1-ferricytochrome c with determination of the formal potentials for the native and chemically-denatured states we have determined the free energy of denaturation of the ferro form of the protein. We report that the simplest of all chemical modifications, addition of an electron, increases the stability of ferricytochrome c by approximately 10 kcal mol-1 at 300 K, pH 4.6. This makes reduced cytochrome c one of the most stable proteins yet investigated.

摘要

通过将酿酒酵母同工酶-1-铁细胞色素c的C102T变体的变性自由能测量值与天然态和化学变性态的形式电位测定相结合，我们确定了该蛋白质亚铁形式的变性自由能。我们报告称，在300K、pH 4.6条件下，所有化学修饰中最简单的一种——添加一个电子，可使铁细胞色素c的稳定性增加约10千卡/摩尔。这使得还原型细胞色素c成为迄今研究的最稳定的蛋白质之一。