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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Insights into the relationship between the haem-binding pocket and the redox potential of c(6) cytochromes: four atomic resolution structures of c(6) and c(6)-like proteins from Synechococcus sp. PCC 7002
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Insights into the relationship between the haem-binding pocket and the redox potential of c(6) cytochromes: four atomic resolution structures of c(6) and c(6)-like proteins from Synechococcus sp. PCC 7002

机译：见解之间的关系haem-binding口袋的氧化还原电势(6)细胞色素c:四个原子分辨率结构的c(6)和c(6)——蛋白质

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摘要

The structure of cytochrome c(6C) from the mesophilic cyanobacterium Synechococcus sp. PCC 7002 has been determined at 1.03 angstrom resolution. This is the first structural report on the recently discovered cyanobacterial cytochrome c(6)-like proteins found in marine and nitrogen-fixing cyanobacteria. Despite high similarity in the overall three-dimensional fold between cytochromes c(6) and c(6C), the latter shows saliently different electrostatic properties in terms of surface charge distribution and dipole moments. Its midpoint redox potential is less than half of the value for typical c(6) cytochromes and results mainly from the substitution of one residue in the haem pocket. Here, high-resolution crystal structures of mutants of both cytochromes c(6) and c(6C) are presented, and the impact of the mutation of specific residues in the haem-binding pocket on the redox potential is discussed. These findings contribute to the elucidation of the structure-function relationship of c(6)-like cytochromes.
机译：细胞色素c的结构(6 c)嗜中温藻青菌聚球藻属PCC sp7002年被确定为1.03埃决议。在蓝藻最近发现细胞色素c(6)——蛋白质在海洋和发现固氮蓝藻。相似度在整个三维折叠之间的细胞色素c(6)和c (6 c),后者显示了近年来不同的静电属性的表面电荷分布和偶极矩。氧化还原电位是不到一半的价值典型的c(6)细胞色素和主要结果替换的一个血红素的残留口袋里。突变体的细胞色素c(6)和c (6 c),并给出了突变的影响特定的残留在haem-binding口袋讨论了氧化还原电位。导致的说明c(6)式的结构关系细胞色素。

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