INVESTIGADORES
VILA Alejandro Jose
artículos
Título:
Mechanism of CuA assembly
Autor/es:
ABRIATA, LA; BANCI, L; BERTINI, I; CIOFI-BAFFONI, S; GKAZONIS, P; SPYROULIAS, G; VILA, AJ; WANG, S
Revista:
Nature Chemical Biology
Editorial:
Nature Publishing Group
Referencias:
Lugar: Washington, USA; Año: 2008 vol. 4 p. 599 - 601
ISSN:
1552-4450
Resumen:
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.
