Characterization of the cytochrome c oxidase assembly factor Cox19 of Saccharomyces cerevisiae

Kevin Rigby, Limei Zhang, Paul A. Cobine, Graham N. George, Dennis R. Winge

Research output: Contribution to journalArticlepeer-review

51 Scopus citations


Cox19 is an important accessory protein in the assembly of cytochrome c oxidase in yeast. The protein is functional when tethered to the mitochondrial inner membrane, suggesting its functional role within the intermembrane space. Cox19 resembles Cox17 in having a twin CX9C sequence motif that adopts a helical hairpin in Cox17. The function of Cox17 appears to be a Cu(I) donor protein in the assembly of the copper centers in cytochrome c oxidase. Cox19 also resembles Cox17 in its ability to coordinate Cu(I). Recombinant Cox19 binds 1 mol eq of Cu(I) per monomer and exists as a dimeric protein. Cox19 isolated from the mitochondrial intermembrane space contains variable quantities of copper, suggesting that Cu(I) binding may be a transient property. Cysteinyl residues important for Cu(I) binding are also shown to be important for the in vivo function of Cox19. Thus, a correlation exists in the ability to bind Cu(I) and in vivo function.

Original languageEnglish (US)
Pages (from-to)10233-10242
Number of pages10
JournalJournal of Biological Chemistry
Issue number14
StatePublished - Apr 6 2007
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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