Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein

Cox11 is a protein essential for respiratory growth and has been implicated in the assembly of the Cu(B) site of cytochrome c oxidase. In the present study, we demonstrate that Cox11 is a copper-binding protein. The soluble C-terminal domain of Cox11 forms a dimer that coordinates one Cu(I) per mono...

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Bibliographic Details
Published in:The Journal of biological chemistry 2002-08, Vol.277 (34), p.31237-31242
Main Authors: Carr, Heather S, George, Graham N, Winge, Dennis R
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
Carrier Proteins - chemistry
Copper - metabolism
Cysteine - metabolism
Dimerization
Electron Transport Complex IV - chemistry
Electron Transport Complex IV - metabolism
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - metabolism
Mitochondrial Proteins
Molecular Sequence Data
Protein Biosynthesis
Protein Conformation
Saccharomyces cerevisiae Proteins
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Summary:Cox11 is a protein essential for respiratory growth and has been implicated in the assembly of the Cu(B) site of cytochrome c oxidase. In the present study, we demonstrate that Cox11 is a copper-binding protein. The soluble C-terminal domain of Cox11 forms a dimer that coordinates one Cu(I) per monomer via three thiolate ligands. The two Cu(I) ions in the dimer exist in a binuclear cluster and appear to be ligated by three conserved Cys residues. Mutation of any of these Cys residues reduces Cu(I) binding and confers respiratory incompetence. Cytochrome c oxidase activity is reduced in these mutants. Thus, the residues important for Cu(I) binding correlate with in vivo function, suggesting that Cu(I) binding is important in Cox11 function.
ISSN:0021-9258
DOI:10.1074/jbc.m204854200