Gene Symbol: COX15
Description: Cox15p
Alias: Cox15p
Species: Saccharomyces cerevisiae S288c
Products:     COX15

Top Publications

  1. Taylor N, Swenson S, Harris N, Germany E, Fox J, Khalimonchuk O. The Assembly Factor Pet117 Couples Heme a Synthase Activity to Cytochrome Oxidase Assembly. J Biol Chem. 2017;292:1815-1825 pubmed publisher
    ..Its synthesis from heme b requires several enzymes, including the evolutionarily conserved heme a synthase (Cox15)...
  2. Barros M, Tzagoloff A. Regulation of the heme A biosynthetic pathway in Saccharomyces cerevisiae. FEBS Lett. 2002;516:119-23 pubmed
    ..This reaction was proposed to be catalyzed by Cox15p, ferredoxin, and ferredoxin reductase. Oxidation of the alcohol to the corresponding aldehyde yields heme A...
  3. Mick D, Wagner K, van der Laan M, Frazier A, Perschil I, Pawlas M, et al. Shy1 couples Cox1 translational regulation to cytochrome c oxidase assembly. EMBO J. 2007;26:4347-58 pubmed
    ..We suggest that Shy1 links Cox1 translational regulation to complex IV assembly and supercomplex formation. ..
  4. Swenson S, Cannon A, Harris N, Taylor N, Fox J, Khalimonchuk O. Analysis of Oligomerization Properties of Heme a Synthase Provides Insights into Its Function in Eukaryotes. J Biol Chem. 2016;291:10411-25 pubmed publisher
    ..evolutionarily conserved enzymes have been implicated in the biosynthesis of heme a, including the heme a synthase Cox15. However, the structure of Cox15 is unknown, its enzymatic mechanism and the role of active site residues remain ..
  5. Barros M, Nobrega F, Tzagoloff A. Mitochondrial ferredoxin is required for heme A synthesis in Saccharomyces cerevisiae. J Biol Chem. 2002;277:9997-10002 pubmed is formed by an initial hydroxylation of the C-8 methyl by a three-component monooxygenase consisting of Cox15p, ferredoxin, and ferredoxin reductase...
  6. Wang Z, Wang Y, Hegg E. Regulation of the heme A biosynthetic pathway: differential regulation of heme A synthase and heme O synthase in Saccharomyces cerevisiae. J Biol Chem. 2009;284:839-47 pubmed publisher
    ..In eukaryotes, two inner mitochondrial membrane proteins, heme O synthase (Cox10) and heme A synthase (Cox15), are required for heme A biosynthesis...
  7. Khalimonchuk O, Bird A, Winge D. Evidence for a pro-oxidant intermediate in the assembly of cytochrome oxidase. J Biol Chem. 2007;282:17442-9 pubmed
    ..A formation but exacerbated by either enhanced Cox1 expression or heme A production arising from overexpression of COX15. Sco1 and Cox11 are implicated in the formation of the Cu(A) and Cu(B) sites of CcO, respectively...
  8. Bestwick M, Khalimonchuk O, Pierrel F, Winge D. The role of Coa2 in hemylation of yeast Cox1 revealed by its genetic interaction with Cox10. Mol Cell Biol. 2010;30:172-85 pubmed publisher
    ..The suppressor activity of N196K mutant Cox10 is dependent on its catalytic function and the presence of Cox15, the second enzyme involved in heme a biosynthesis...
  9. Glerum D, Muroff I, Jin C, Tzagoloff A. COX15 codes for a mitochondrial protein essential for the assembly of yeast cytochrome oxidase. J Biol Chem. 1997;272:19088-94 pubmed
    ..This gene is identical to reading frame YER141w on chromosome 5. To facilitate further studies, Cox15p has been expressed as a biotinylated protein...

More Information


  1. Barros M, Carlson C, Glerum D, Tzagoloff A. Involvement of mitochondrial ferredoxin and Cox15p in hydroxylation of heme O. FEBS Lett. 2001;492:133-8 pubmed
    b>Cox15p is essential for the biogenesis of cytochrome oxidase [Glerum et al., J. Biol. Chem. 272 (1997) 19088-19094]. We show here that cox15 mutants are blocked in heme A but not heme O biosynthesis...
  2. Bareth B, Dennerlein S, Mick D, Nikolov M, Urlaub H, Rehling P. The heme a synthase Cox15 associates with cytochrome c oxidase assembly intermediates during Cox1 maturation. Mol Cell Biol. 2013;33:4128-37 pubmed publisher
    ..Shy1, the yeast SURF1 homolog, has been implicated in heme transfer to Cox1, whereas the heme a synthase, Cox15, catalyzes the final step of heme a synthesis...