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• W2035598432 abstract "Mitochondrial cytochrome c oxidase is a key protonmotive component of the respiratory chain. Mutations in the mitochondrially‐encoded subunits of the complex have been reported in association with a range of diseases. In this work we used yeast and bacterial mutants to assess the effect of human mutations in subunit 1 (L196I) and subunit 3 (G78S, A200T, ΔF94–F98, F251L and W249Stop). While the stop mutation at the C‐terminus of subunit 3 and the short deletion were highly deleterious and abolished the assembly of the mitochondrial enzyme, the four missense mutations caused little or no effect on the respiratory function. Detailed analysis of G78S, A200T and ΔF94–F98 in Rhodobacter sphaeroides confirmed and extended these observations. We show in this study that the combination of yeast and bacterial models is a useful tool to elucidate the effect of mutations in the catalytic core of cytochrome oxidase. The yeast enzyme is highly similar to the human enzyme and provides a good model to assess the deleterious effect of reported mutations. The bacterial system allows detailed biochemical analysis of the effect of the mutations on the function and assembly of the catalytic core of the enzyme." @default.
• W2035598432 created "2016-06-24" @default.
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• W2035598432 date "2003-02-24" @default.
• W2035598432 modified "2023-10-17" @default.
• W2035598432 title "Disease-related mutations in cytochrome c oxidase studied in yeast and bacterial models" @default.
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• W2035598432 doi "https://doi.org/10.1046/j.1432-1033.2003.03482.x" @default.
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