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.
Mechanism of Cu(A) assembly / L.A.Abriata; L.Banci; I.Bertini; S.Ciofi-Baffoni; P.Gkazonis; G.A.Spyroulias; A.J.Vila; S.Wang. - In: NATURE CHEMICAL BIOLOGY. - ISSN 1552-4450. - STAMPA. - 4:(2008), pp. 599-601. [10.1038/nchembio.110]
Mechanism of Cu(A) assembly
BANCI, LUCIA;BERTINI, IVANO;CIOFI BAFFONI, SIMONE;WANG, SHENLIN
2008
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.
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