IBR 13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
artículos
Título:
Mechanism of CuA assembly
Autor/es:
LUCIANO A ABRIATA; LUCIA BANCI; IVANO BERTINI; SIMONE CIOFI-BAFFONI; PETROS GKAZONIS; GEORGIOS A SPYROULIAS; ALEJANDRO J VILA; SHENLIN WANG
Revista:
Nature Chemical Biology
Referencias:
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 (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.
