Molecular coevolution of the vertebrate cytochrome c(1) and Rieske iron sulphur protein in the cytochrome bc(1) complex.
Cytochrome c(1) (cyt-c(1)) and the Rieske Iron Sulphur Protein (ISP) are subunits of the cytochrome bc(1) 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-c(1) 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-c(1). There is evidence supporting coevolution of these proteins relative to alpha helical tendencies, compressibility and equilibrium constant.
Department of Integrative Biology, Brigham Young University, Provo, UT 84602, USA. kimberly.baer@gmail.com
Kimberly K
KK
Baer
David A
DA
McClellan
D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D001671:Biochemistry / Q000379:methods; D019295:Computational Biology; D003575:Cytochromes c1 / Q000737:chemistry*; D004579:Electron Transport; D014450:Electron Transport Complex III / Q000737:chemistry*; D004583:Electrons; D006801:Humans; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008968:Molecular Conformation; D010802:Phylogeny; D011487:Protein Conformation; D011522:Protons; D014451:Ubiquinone / Q000737:chemistry
D000596:Amino Acids; D007506:Iron-Sulfur Proteins; D011522:Protons; C037989:Rieske iron-sulfur protein; D014451:Ubiquinone; D003575:Cytochromes c1; D014450:Electron Transport Complex III