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

摘要

Homogeneous and heterogeneous electron transfer proceses associated with the c-type cytochromes have bee widely studied because such studies can yield improtant information not only about thermodyunamic, kinetic and structural properties of the proteins, but also provide novel insights into the electron transfer mechanism of the proteins in vivo~(1-3), The emergency of molecular genertic techniques provided an opportunity to study a variety of spectroscopic properties on the structure basis and the correlation between the elctron transfer and structure of the protein in such a sdesigned way taht the sturcture of the proteins can be specifically modified. In this paper , attention was mainly focused on the effect of this mutation on the stability and redox properties of yeast iso-1-cytochrome c (WT) and its mutant F82H.