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PMID: 18758441 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Mechanism of Cu(A) assembly.

Nature chemical biology ·Vol. 4 ·No. 10 ·2008-10-00 ·Pages 599-601

Abriata LA, Banci L, Bertini I, Ciofi-Baffoni S, Gkazonis P, Spyroulias GA, Vila AJ, Wang S

Abstract

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 (PCu(A)C) 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 Cu(A) cysteine ligands.

MeSH Terms
Copper/physiology Electron Transport Complex IV/physiology Models, Molecular Oxidation-Reduction Thermus thermophilus/enzymology
Chemicals
Copper Electron Transport Complex IV
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Abriata Luciano A
Instituto de Biología Molecular y Celular de Rosario, Consejo Nacional de Investigaciones Científicas y Técnicas, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 531, (S2002LRK) Rosario, Argentina.
Banci Lucia
Bertini Ivano
Ciofi-Baffoni Simone
Gkazonis Petros
Spyroulias Georgios A
Vila Alejandro J
Wang Shenlin
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21 references, click to expand
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Article Info
Journal
Nature chemical biology
Abbr.
Nat Chem Biol
ISSN
1552-4469
DOI
10.1038/nchembio.110
Published
2008-10-00
Epub
2008-00-31
Pages
599-601
Language
English
Region
United States
NLM ID
101231976
PMCID
PMC2596924
Subset
IM
Grants
NIGMS NIH HHS · R01 GM068682 · United States
NIGMS NIH HHS · R01 GM068682-03 · United States
NIGMS NIH HHS · R01-GM068682 · United States
Howard Hughes Medical Institute · United States
External Links
PubMed source DOI: 10.1038/nchembio.110 PMC Full Text View journal details
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