Molecular coevolution of the vertebrate cytochrome c1 and Rieske Iron Sulphur Protein in the cytochrome bc1 complex. (16th October 2007)

• Record Type: Journal Article
• Authors: Baer, Kimberly K.; McClellan, David A.
• Is Part Of: International journal of bioinformatics research and applications. Volume 3:Number 4(2007)
• Page Start: 456
• Page End: 470
• Publication Date: 2007-10-16
• Subjects: molecular coevolution -- cytochrome c1 -- Rieske iron sulphur protein -- ISP -- cytochrome bc1 complex -- biochemical adaptation -- bioinformatics -- vertebrate cytochrome -- mitochondria -- protein structure -- model organism phylogenies; Bioinformatics -- Periodicals; 570.285
• Languages: English
• ISSNs: 1744-5485

Abstract

Cytochrome c1 (cyt-c1) and the Rieske Iron Sulphur Protein (ISP) are subunits of the cytochrome bc1 complex located in the mitochondria functioning both as a proton pump and an electron transporter. Vertebrate model organism phylogenies were used in conjunction with existing 3D protein structures to evaluate the biochemical evolution of cyt-c1 and ISP in terms of selection on amino acid properties. We found selection acting on the exterior surfaces of both proteins and specifically the core region of cyt-c1. There is evidence supporting coevolution of these proteins relative to alpha helical tendencies, compressibility and equilibrium constant.