THE STRUCTURE OF FLAVOCYTOCHROME-C SULFIDE DEHYDROGENASE FROM A PURPLE PHOTOTROPHIC BACTERIUM
THE STRUCTURE OF FLAVOCYTOCHROME-C SULFIDE DEHYDROGENASE FROM A PURPLE PHOTOTROPHIC BACTERIUM
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DOI：
10.1126/science.7939681
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发表时间：
1994-10-21
期刊：
影响因子：
56.9
通讯作者：
MATHEWS, FS
中科院分区：
文献类型：
--
作者：
CHEN, ZW;KOH, M;MATHEWS, FS
以2.53埃的分辨率测定了铬酸盐黄细胞色素硫化物脱氢酶的异二聚体结构。它含有谷胱甘肽还原酶样黄素结合亚基和二血红素细胞色素亚基。二血红素细胞色素折叠成两个结构域，每个结构域类似于线粒体细胞色素c，并且在亚基内部有一个不寻常的丙酸间连接，将两个血红素基团连接在一起。黄素蛋白亚基的活性位点包含一个位于黄素环嘧啶部分上方的具有重要催化作用的二硫桥。色氨酸、苏氨酸或酪氨酸侧链可以为电子转移到距离黄素10埃的血红素基团之一提供部分通道。
The structure of the heterodimeric flavocytochrome c sulfide dehydrogenase from Chromatium vinosum was determined at a resolution of 2.53 angstroms. It contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit. The diheme cytochrome folds as two domains, each resembling mitochondrial cytochrome c, and has an unusual interpropionic acid linkage joining the two heme groups in the interior of the subunit. The active site of the flavoprotein subunit contains a catalytically important disulfide bridge located above the pyrimidine portion of the flavin ring. A tryptophan, threonine, or tyrosine side chain may provide a partial conduit for electron transfer to one of the heme groups located 10 angstroms from the flavin.