Abstract
Assembly of functional cytochrome oxidase in yeast requires Cox17, which has been postulated to deliver copper ions to the mitochondrion for insertion into the enzyme. This role for Cox17 is supported by the observation that it binds copper as a binuclear cuprous-thiolate cluster. X-ray absorption spectroscopy, together with UV-visible absorption and emission spectroscopy, indicates the presence of bound cuprous ions, trigonally coordinated by thiolate ligands. Analysis of the EXAFS shows three Cu-S bonds at 2.26 A, plus a short Cu-Cu distance of 2.7 A, indicating a binuclear cluster in Cox17. The cuprous-thiolate cluster in Cox17 is substantially more labile than structurally related clusters in metallothioneins.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics
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Cation Transport Proteins*
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Copper / chemistry*
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Copper Transport Proteins
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Electron Transport Complex IV / chemistry*
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Electron Transport Complex IV / genetics
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Fourier Analysis
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Fungal Proteins / chemistry
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Fungal Proteins / genetics
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Genes, Synthetic
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Luminescent Measurements
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Molecular Chaperones
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Proteins / chemistry*
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Proteins / genetics
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins*
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Spectrometry, X-Ray Emission
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Spectrophotometry, Ultraviolet
Substances
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COX17 protein, S cerevisiae
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Carrier Proteins
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Cation Transport Proteins
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Copper Transport Proteins
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Fungal Proteins
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Molecular Chaperones
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Proteins
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Saccharomyces cerevisiae Proteins
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Copper
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Electron Transport Complex IV