Corresponding Author

Jun wei ZHENG


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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