Molecular coevolution of the vertebrate cytochrome c(1) and Rieske iron sulphur protein in the cytochrome bc(1) complex.
Molecular coevolution of the vertebrate cytochrome c(1) and Rieske iron sulphur protein in the cytochrome bc(1) complex.
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DOI：
10.1504/ijbra.2007.015414
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发表时间：
2007-01-01
影响因子：
--
通讯作者：
McClellan, David A
中科院分区：
文献类型：
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作者：
Baer, Kimberly K;McClellan, David A
细胞色素c(1) （cyt-c(1)）和Rieske铁硫蛋白（ISP）是细胞色素bc(1)复合物的亚基，位于线粒体中，具有质子泵和电子转运体的功能。我们将脊椎动物模式生物系统发育与现有的3D蛋白质结构结合起来，评估了cyt-c(1)和ISP在氨基酸特性选择方面的生化进化。我们发现选择作用于两种蛋白质的外表面，特别是cyt-c的核心区域(1)。有证据支持这些蛋白质的共同进化相对于α螺旋倾向，可压缩性和平衡常数。
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.