Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Regular Papers
Correlation between the Stability and Redox Potential of Three Homologous Cytochromes c from Two Thermophiles and One Mesophile
Taku TAKEDATakafumi SONOYAMAShin-ichi J. TAKAYAMAHajime MITAYasuhiko YAMAMOTOYoshihiro SAMBONGI
Author information
JOURNAL FREE ACCESS

2009 Volume 73 Issue 2 Pages 366-371

Details
Abstract

The stability of the oxidized and reduced forms of three homologous cytochromes c from two thermophiles and one mesophile was systematically monitored by means of Soret absorption measurements in the presence of various concentrations of a denaturant, guanidine thiocyanate, at pH 7.0 at 25 °C. Thermophilic Hydrogenobacter thermophilus cytochrome c552 was the most stable in both redox states, followed by moderately thermophilic Hydrogenophilus thermoluteolus cytochrome c552, and then mesophilic Pseudomonas aeruginosa cytochrome c551. Further stability and electrochemical analysis of the three proteins and the reciprocal variants, which exhibited a different hydrophobic interaction with the heme, showed that the one with the higher stability in both redox states had the lower redox potential. Consequently, these cytochromes c probably adapted to the cellular environments of the original bacteria with correlated stability and redox potential constraints, which are in part regulated by the hydrophobicity around the heme.

Content from these authors

This article cannot obtain the latest cited-by information.

© 2009 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
Previous article Next article
feedback
Top