Title: Molecular coevolution of the vertebrate cytochrome c₁ and Rieske Iron Sulphur Protein in the cytochrome bc₁ complex

Authors: Kimberly K. Baer, David A. McClellan

Addresses: Department of Integrative Biology, Brigham Young University, Provo, UT 84602, USA. ' Department of Integrative Biology, Brigham Young University, Provo, UT 84602, USA

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.

Keywords: molecular coevolution; cytochrome c₁; Rieske iron sulphur protein; ISP; cytochrome bc₁ complex; biochemical adaptation; bioinformatics; vertebrate cytochrome; mitochondria; protein structure; model organism phylogenies.

DOI: 10.1504/IJBRA.2007.015414

International Journal of Bioinformatics Research and Applications, 2007 Vol.3 No.4, pp.456 - 470

Published online: 15 Oct 2007 *

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