Molecular coevolution of the vertebrate cytochrome c₁ and Rieske Iron Sulphur Protein in the cytochrome bc₁ complex
by Kimberly K. Baer, David A. McClellan
International Journal of Bioinformatics Research and Applications (IJBRA), Vol. 3, No. 4, 2007

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.

Online publication date: Mon, 15-Oct-2007

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