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
中科院分区:
文献类型:
--
作者:
Nyvltova, Eva;Dietz, Jonathan V.;Seravalli, Javier;Khalimonchuk, Oleh;Barrientos, Antoni
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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影响因子:
29
作者:
De Silva D;Fontanesi F;Barrientos A
通讯作者:
Barrientos A
DOI:
10.1073/pnas.0800019105
发表时间:
2008-05-13
影响因子:
11.1
作者:
Banci, Lucia;Bertini, Ivano;Palumaa, Peep
通讯作者:
Palumaa, Peep
影响因子:
4.8
作者:
Bourens, Myriam;Barrientos, Antoni
通讯作者:
Barrientos, Antoni
影响因子:
3.5
作者:
D'Aurelio, Marilena;Gajewski, Carl D.;Manfredi, Giovanni
通讯作者:
Manfredi, Giovanni
影响因子:
3.5
作者:
Barros, MH;Tzagoloff, A
通讯作者:
Tzagoloff, A