Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum.
Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum.
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寄生线虫猪蛔虫线粒体喹啉-富马酸还原酶的晶体结构。
DOI：
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发表时间：
2012
期刊：
影响因子：
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通讯作者：
K. Kita
中科院分区：
文献类型：
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作者：
H. Shimizu;A. Osanai;K. Sakamoto;D. Inaoka;T. Shiba;S. Harada;K. Kita
在猪蛔虫的厌氧呼吸链中，复合体II将富马酸的还原与对苯二酚的氧化偶联，后者是哺乳动物复合体II催化的反向反应。该结构由四个亚基和五个辅助因子组成，除了在猪链霉菌酶的最小锚定亚基中发现了一个额外的多肽外，与有氧复合体II的结构相似。在此，我们讨论了该酶的结构与功能的关系，以及在反丁烯二酸还原猪链霉菌复合体II的过程中，罗丹酚的低氧化还原电位所起的关键作用。
In the anaerobic respiratory chain of the parasitic nematode Ascaris suum, complex II couples the reduction of fumarate to the oxidation of rhodoquinol, a reverse reaction catalyzed by mammalian complex II. In this study, the first structure of anaerobic complex II of mitochondria was determined. The structure, composed of four subunits and five co-factors, is similar to that of aerobic complex II, except for an extra peptide found in the smallest anchor subunit of the A. suum enzyme. We discuss herein the structure-function relationship of the enzyme and the critical role of the low redox potential of rhodoquinol in the fumarate reduction of A. suum complex II.