Serrs and Electrochemical Study of Yeast Iso-1-Cytochrome c Mutant F82H

应用表面增强拉曼光谱和循环伏安法研究了细胞色素c及其突变体F82H的氧化还原性质 .结果表明苯丙氨酸对组氨酸的取代使得蛋白质结构更为稳定 .相对于原体蛋白质 ,突变体的氧化还原电位向负电位方向移动 ,这被归因于由氧化还原过程中伴随有配体转换反应影响所致 .The redox properties of iso?1?yeast cytochrome c and its mutant F82H were studied by surface?enhanced Raman spectroscopy and cyclic voltammetry. The results showed that the replacement of phenylalanine?82 with histidine led to a more stable global structure of the protein. A negative shift in the redox potential of the mutant relative to that of wild type protein is ascribed to a ligand switching reaction during the redox processes.作者联系地址：苏州大学化学系!江苏苏州215006,苏州大学化学系!江苏苏州215006,中国科学院长春应用化学研究所!吉林长春130022,Dept.of Chem.!Iowa State Univ.,Ames,IA50011,USA,Dept.of Chem.!Iowa State Univ.,Ames,IA50011,USAAuthor's Address: 1. Dept. of Chem., Suzhou Univ., Suzhou 215006, China; 2. Inst. of Changchun Applied Chem.,Chinese Academy of Sci.,Changchun 130022, China; 3. Dept.