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Structural insights into electron transfer in caa_3-type cytochrome oxidase

机译:Caa_3型细胞色素氧化酶中电子转移的结构见解

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摘要

Cytochrome c oxidase is a member of the haem copper oxidase superfamily (HCO)~1. HCOs function as the terminal enzymes in the respiratory chain of mitochondria and aerobic prokaryotes, coupling molecular oxygen reduction to transmembrane proton pumping. Integral to the enzyme's function is the transfer of electrons from cytochrome c to the oxidase via a transient association of the two proteins. Electron entry and exit are proposed to occur from the same site on cytochrome c~(2-4). Here we report the crystal structure of the caa_3-type cytochrome oxidase from Thermus thermophilus, which has a covalently tethered cytochrome c domain. Crystals were grown in a bicontinuous mesophase using a synthetic short-chain monoacylglycerol as the hosting lipid. From the electron density map, at 2.36 A resolution, a novel integral membrane subunit and a native glycoglycerophospholipid embedded in the complex were identified. Contrary to previous electron transfer mechanisms observed for soluble cytochrome c, the structure reveals the architecture of the electron transfer complex for the fused cupredoxin/ cytochrome c domain, which implicates different sites on cytochrome c for electron entry and exit. Support for an alternative to the classical proton gate characteristic of this HCO class is presented.
机译:细胞色素c氧化酶是血红素铜氧化酶超家族(HCO)〜1的成员。 HCOs充当线粒体和有氧原核生物呼吸链中的末端酶,将分子氧还原与跨膜质子泵送耦合。该酶功能不可或缺的是电子通过两种蛋白质的瞬时缔合从细胞色素c转移到氧化酶。提出电子进入和离开都发生在细胞色素c〜(2-4)的同一位置。在这里,我们报告了嗜热栖热菌的caa_3型细胞色素氧化酶的晶体结构,该晶体结构具有共价连接的细胞色素c结构域。使用合成的短链单酰基甘油作为宿主脂质,晶体在双连续中间相中生长。从电子密度图,在2.36 A的分辨率,确定了一个新的完整的膜亚基和复合物中嵌入的天然糖甘油磷脂。与先前针对可溶性细胞色素c观察到的电子转移机制相反,该结构揭示了融合的铜氧还蛋白/细胞色素c结构域的电子转移复合物的结构,这暗示了细胞色素c上电子进入和离开的不同位点。提出了对该HCO类经典质子门特性的替代方法的支持。

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  • 来源
    《Nature》 |2012年第7408期|p.514-518|共5页
  • 作者单位

    Department of Chemical and Environmental Sciences, University of Limerick, Limerick, Ireland,School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland;

    School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland,Australian Synchrotron,800 Blackburn Road, Clayton, Victoria 3168, Australia;

    Department of Chemical and Environmental Sciences, University of Limerick, Limerick, Ireland;

    Theoretical Biochemistry Laboratory, RIKEN Advanced Science Institute, Wako, Saitama 351-0198, Japan;

    Department of Chemical and Environmental Sciences, University of Limerick, Limerick, Ireland,Materials and Surface Science Institute,University of Limerick, Limerick, Ireland;

    School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland,School of Medicine, Trinity College Dublin, Dublin, Ireland;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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