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Mechanism of Cu(A) assembly.

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.

SUBMITTER: Abriata LA

PROVIDER: S-EPMC2596924 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature

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Mechanism of Cu(A) assembly.

Abriata Luciano A LA Banci Lucia L Bertini Ivano I Ciofi-Baffoni Simone S Gkazonis Petros P Spyroulias Georgios A GA Vila Alejandro J AJ Wang Shenlin S

Nature chemical biology 20080831 10

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 ligand ...[more]

PMID: 18758441

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