CRYSTAL-STRUCTURE OF A COMPLEX BETWEEN ELECTRON-TRANSFER PARTNERS, CYTOCHROME-C PEROXIDASE AND CYTOCHROME-C
CRYSTAL-STRUCTURE OF A COMPLEX BETWEEN ELECTRON-TRANSFER PARTNERS, CYTOCHROME-C PEROXIDASE AND CYTOCHROME-C
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DOI：
10.1126/science.1334573
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发表时间：
1992-12-11
期刊：
影响因子：
56.9
通讯作者：
KRAUT, J
中科院分区：
文献类型：
--
作者：
PELLETIER, H;KRAUT, J
酵母细胞色素 c 过氧化物酶和酵母 iso-1-细胞色素 c 之间的 1:1 复合物的晶体结构以 2.3 埃分辨率测定。这种结构揭示了一种可能的电子转移途径，与之前针对这种广泛研究的氧化还原对提出的任何途径不同。两个血红素之间的最短直线紧密遵循残基 Ala194、Ala193、Gly192 和最后的 Trp191 的过氧化物酶主链，其吲哚环垂直于过氧化物酶血红素，并与过氧化物酶血红素进行范德华接触。还测定了酵母细胞色素c过氧化物酶和马心细胞色素c之间的复合物在2.8埃处的晶体结构。尽管这两种复合物（一种含有来自酵母的细胞色素 c，另一种含有来自马的细胞色素 c）的晶体在非常不同的条件下生长并且属于不同的空间群，但这两种复合物的结构非常相似，表明细胞色素 c 以高度特异性的方式与其氧化还原伙伴相互作用。
The crystal structure of a 1:1 complex between yeast cytochrome c peroxidase and yeast iso-1-cytochrome c was determined at 2.3 angstrom resolution. This structure reveals a possible electron transfer pathway unlike any previously proposed for this extensively studied redox pair. The shortest straight line between the two hemes closely follows the peroxidase backbone chain of residues Ala194, Ala193, Gly192, and finally Trp191, the indole ring of which is perpendicular to, and in van der Waals contact with, the peroxidase heme. The crystal structure at 2.8 angstrom of a complex between yeast cytochrome c peroxidase and horse heart cytochrome c was also determined. Although crystals of the two complexes (one with cytochrome c from yeast and the other with cytochrome c from horse) grew under very different conditions and belong to different space groups, the two complex structures are closely similar, suggesting that cytochrome c interacts with its redox partners in a highly specific manner.