Mechanism of CuA assembly

被引：105

作者：

Abriata, Luciano A. ^{[1
,2
,3
]}

Banci, Lucia ^{[1
,2
]}

Bertini, Ivano ^{[1
,2
]}

Ciofi-Baffoni, Simone ^{[1
,2
]}

Gkazonis, Petros ^{[1
,2
,4
]}

Spyroulias, Georgios A. ^{[4
]}

Vila, Alejandro J. ^{[3
]}

Wang, Shenlin ^{[1
,2
]}

机构：

[1] Univ Florence, Magnet Resonance Ctr CERM, I-50019 Florence, Italy

[2] Univ Florence, Dept Chem, I-50019 Florence, Italy

[3] Univ Nacl Rosario, Inst Mol & Cellular Biol Rosario, Consejo Nacl Invest Cient & Tecn, Fac Ciencias Bioquim & Farmaceut, RA-2000 Rosario, Argentina

[4] Univ Patras, Dept Pharm, GR-26504 Patras, Greece

来源：

NATURE CHEMICAL BIOLOGY | 2008年 / 4卷 / 10期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1038/nchembio.110

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Copper is essential for proper functioning of cytochrome c oxidases, and therefore for cellular respiration in eukaryotes and many bacteria. Here we show that a new periplasmic protein (PCuAC) selectively inserts Cu(I) ions into subunit II of Thermus thermophilus ba(3) oxidase to generate a native Cu-A site. The purported metallochaperone Sco1 is unable to deliver copper ions; instead, it works as a thiol-disulfide reductase to maintain the correct oxidation state of the CuA cysteine ligands.

引用

页码：599 / 601

页数：3

共 22 条

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