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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 cytochrome c and its mutant F82H were studied by surface enhanced Raman spectroscopy and cyclic voltammetry.The results showed that the substitution of histidine for phenylalanine made the protein structure more stable.Compared with the protoplast protein , The redox potential of the mutant shifted to the negative potential due to the concomitant effect of the ligand conversion reaction during the redox process.