Abriata Luciano A, Banci Lucia, Bertini Ivano, Ciofi-Baffoni Simone, Gkazonis Petros, Spyroulias Georgios A, Vila Alejandro J, Wang Shenlin
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.
Nat Chem Biol. 2008 Oct;4(10):599-601. doi: 10.1038/nchembio.110. Epub 2008 Aug 31.
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.
铜对于细胞色素c氧化酶的正常功能至关重要,因此对于真核生物和许多细菌中的细胞呼吸也至关重要。在此我们表明,一种新的周质蛋白(PCu(A)C)可将Cu(I)离子选择性地插入嗜热栖热菌ba(3)氧化酶的亚基II中,以生成天然的Cu(A)位点。所谓的金属伴侣蛋白Sco1无法传递铜离子;相反,它作为一种硫醇-二硫键还原酶,以维持Cu(A)半胱氨酸配体的正确氧化态。