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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain.
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The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain.

机译：1.2人类亚硫酸盐氧化酶的结构细胞色素b(5)域。

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摘要

The molybdenum- and iron-containing enzyme sulfite oxidase catalyzes the physiologically vital oxidation of sulfite to sulfate. Sulfite oxidase contains three domains: an N-terminal cytochrome b(5) domain, a central domain harboring the molybdenum cofactor (Moco) and a C-terminal dimerization domain. Oxidation of the substrate sulfite is coupled to the transfer of two electrons to the molybdenum cofactor. Subsequently, these electrons are passed on, one at a time, to the b(5) heme of sulfite oxidase and from there to the soluble electron carrier cytochrome c. The crystal structure of the oxidized human sulfite oxidase cytochrome b(5) domain has been determined at 1.2 A resolution and has been refined to a crystallographic R factor of 0.107 (R(free) = 0.137). A comparison of this structure with other b(5)-type cytochromes reveals distinct structural features present in the sulfite oxidase b(5) domain which promote optimal electron transport between the Moco of sulfite oxidase and the heme of cytochrome c.
机译：钼-和含铁酶亚硫酸盐氧化酶催化生理上至关重要亚硫酸盐氧化硫酸。包含三个领域:一个氨基端细胞色素b(5)领域,中央域窝藏钼辅因子(岩豚鼠)和c端二聚作用域。亚硫酸盐是耦合的两个的转移电子钼辅因子。随后,这些电子传递,一个一次,亚硫酸盐氧化酶的b(5)血红素并从那里可溶性电子载体细胞色素c的晶体结构人类亚硫酸盐氧化酶氧化细胞色素b (5)域已经确定在1.2一项决议并已精制结晶R0.107倍(R(免费)= 0.137)。这个结构与其他b(5)类型细胞色素揭示了不同的结构特点在亚硫酸盐氧化酶(5)域促进之间的最优电子传递墨客亚硫酸盐氧化酶和血红素细胞色素c。

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