Abstract
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.
Publication Date
2001-02-28
Online Available Date
2001-02-28
Revised Date
2001-02-28
Received Date
2001-02-28
Recommended Citation
Jun-wei ZHENG, Re nao GU, Tian hong LU, Chumanov George, M. Cotton Therese.
Serrs and Electrochemical Study of Yeast Iso-1-Cytochrome c Mutant F82H[J]. Journal of Electrochemistry,
2001
,
7(1): Article 16.
DOI: 10.61558/2993-074X.3236
Available at:
https://jelectrochem.xmu.edu.cn/journal/vol7/iss1/16
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