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

Authors

Jun-wei ZHENG, Dept. of Chem., Suzhou Univ., Suzhou 215006, China;
Re nao GU, Dept. of Chem., Suzhou Univ., Suzhou 215006, China;
Tian hong LU, Inst. of Changchun Applied Chem.,Chinese Academy of Sci.,Changchun 130022, China;
Chumanov George, Dept. o;
M. Cotton Therese, Dept. o;

Corresponding Author

Jun wei ZHENG

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.

DOI Link

https://doi.org/10.61558/2993-074X.3236

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