Coordination of metal center biogenesis in human cytochrome c oxidase.

Coordination of metal center biogenesis in human cytochrome c oxidase.
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DOI:
10.1038/s41467-022-31413-1
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发表时间:
2022-06-24
影响因子:
16.6
通讯作者:
Barrientos, Antoni
Barrientos, Antoni
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Nyvltova, Eva;Dietz, Jonathan V.;Seravalli, Javier;Khalimonchuk, Oleh;Barrientos, Antoni

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线粒体细胞色素c氧化酶(CcO)或呼吸链复合物IV是一种血红素aa 3-铜氧还原酶,含有由亚基特异性金属伴侣组装的全复合物生物合成和酶功能所必需的金属中心。该酶具有位于催化核心亚基中的两个铜位点。COX 1亚基含有与血红素a3紧密结合的CuB位点,而COX 2亚基含有双核CuA位点。在这里,我们报告说,在人类细胞中的CcO铜分子伴侣形成大分子组件和合作的几个双CX 9 C蛋白控制血红素的生物合成和协调铜转移顺序的CuA和CuB网站。CcO的这些数据说明了一种机制,调节生物合成的大分子酶组装与几个催化金属氧化还原中心,并防止积累的细胞毒性反应组装中间体。线粒体细胞色素c氧化酶是一种血红素aa 3-铜氧还原酶。在这里,作者报告说,金属中心特异性金属伴侣形成动态组件,以控制血红素a的生物合成和协调铜转移到铜网站。
Mitochondrial cytochrome c oxidase (CcO) or respiratory chain complex IV is a heme aa3-copper oxygen reductase containing metal centers essential for holo-complex biogenesis and enzymatic function that are assembled by subunit-specific metallochaperones. The enzyme has two copper sites located in the catalytic core subunits. The COX1 subunit harbors the CuB site that tightly associates with heme a3 while the COX2 subunit contains the binuclear CuA site. Here, we report that in human cells the CcO copper chaperones form macromolecular assemblies and cooperate with several twin CX9C proteins to control heme a biosynthesis and coordinate copper transfer sequentially to the CuA and CuB sites. These data on CcO illustrate a mechanism that regulates the biogenesis of macromolecular enzymatic assemblies with several catalytic metal redox centers and prevents the accumulation of cytotoxic reactive assembly intermediates. Mitochondrial cytochrome c oxidase is a heme aa3-copper oxygen reductase. Here, authors report that metal center-specific metallochaperones form dynamic assemblies to control heme a biosynthesis and coordinate copper transfer to the copper sites.
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发表时间: 2013-11-05
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影响因子: 29
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发表时间: 2002-04-10
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影响因子: 3.5
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