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 .
郑军伟
,
顾仁敖
,
陆天虹
,
George Chumanov
. 细胞色素c突变体F82H的表面增强拉曼和电化学研究(英文)[J]. 电化学, 2001
, 7(1)
: 37
-40
.
DOI: 10.61558/2993-074X.3236
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.
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