Santucci R, Brunori M, Ascoli F
Biochim Biophys Acta. 1987 Aug 5;914(2):185-9. doi: 10.1016/0167-4838(87)90062-8.
A circular dichroism study of carboxymethylated cytochrome c has been performed to obtain further information on the structural basis responsible for the observed changes in ligand binding and redox properties of the modified cytochrome c. The results give additional evidence of local structural changes occurring in the heme environment upon rupture of the (Met-80)-heme iron bond in the modified protein. This produces no alterations of the overall molecular conformation, but results in drastic changes in redox potential. In addition, analysis of the reversible conformational transitions induced by urea in the native and the modified proteins supports the idea that the modified derivative can be considered as an 'intermediate state' between the native and the fully unfolded protein.
对羧甲基化细胞色素c进行了圆二色性研究，以获取更多有关导致修饰后的细胞色素c在配体结合和氧化还原特性方面所观察到变化的结构基础的信息。结果进一步证明，修饰后的蛋白质中（Met-80）-血红素铁键断裂后，血红素环境发生了局部结构变化。这并未改变整体分子构象，但导致了氧化还原电位的剧烈变化。此外，对天然蛋白质和修饰蛋白质中由尿素诱导的可逆构象转变的分析支持了这样一种观点，即修饰后的衍生物可被视为天然蛋白质和完全展开蛋白质之间的“中间状态”。
