Brief Communication abstract
Nature Chemical Biology 4, 599 - 601 (2008)
Published online: 31 August 2008 | doi:10.1038/nchembio.110
Mechanism of CuA assembly
Luciano A Abriata1,2, Lucia Banci2, Ivano Bertini2, Simone Ciofi-Baffoni2, Petros Gkazonis2,3, Georgios A Spyroulias3, Alejandro J Vila1 & Shenlin Wang2
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 ba3 oxidase to generate a native CuA 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.
- 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.
- Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Scientific Campus, 50019, Sesto Fiorentino, Florence, Italy.
- Department of Pharmacy, University of Patras, Panepistimioupoli-Rion, GR-26504 Patras, Greece.
Correspondence to: Ivano Bertini2 e-mail: ivanobertini@cerm.unifi.it
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