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

Authors

Jun-wei ZHENG, Dept. of Chem., Suzhou Univ., Suzhou 215006, ChinaFollow
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. of Chem., Iowa State Univ., Ames, IA 50011, USA
M. Cotton Therese, Dept. of Chem., Iowa State Univ., Ames, IA 50011, USA

Corresponding Author

Jun-wei ZHENG(jwzheng@suda.edu.cn)

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.

Keywords

Cytochrome c, Mutant, Surface-enhanced Raman spectroscopy

DOI Link

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

Publication Date

2001-02-28

Online Available Date

2001-02-28

Revised Date

2001-02-20

Received Date

2000-11-08

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): 37-40.
DOI: 10.61558/2993-074X.3236
Available at: https://jelectrochem.xmu.edu.cn/journal/vol7/iss1/16