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• W2109512882 abstract "Significance Cellular respiration in humans depends on the correct assembly of a copper site (Cu A ) in cytochrome oxidases. Because copper is toxic at high levels, cells require specific mechanisms to regulate copper transport and delivery. Two proteins from the Sco family are involved in this mechanism in human mitochondria, and mutations on any of these proteins jeopardize the assembly of the Cu A site, leading to lethal pathologies in newborns. We show that Sco1 is a protein responsible for delivering the copper ions to the oxidase, with a high degree of selectivity. Sco2, instead, provides electrons to reduce the nonmetallated site of the oxidase. This evidence allow us to propose a mechanism for assembly of the Cu A site in eukaryotes." @default.
• W2109512882 created "2016-06-24" @default.
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• W2109512882 date "2015-09-08" @default.
• W2109512882 modified "2023-10-11" @default.
• W2109512882 title "Loop recognition and copper-mediated disulfide reduction underpin metal site assembly of Cu _A in human cytochrome oxidase" @default.
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• W2109512882 doi "https://doi.org/10.1073/pnas.1505056112" @default.
• W2109512882 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4586878" @default.
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