Characterization of the Cytochrome C Oxidase Assembly Factor Cox19 of 'Saccharomyces Cerevisiae'

Journal Article · Thu Jul 12 04:00:00 EDT 2007 · J.Biol.Chem.282:10233-10242,2007

DOI:https://doi.org/10.1074/jbc.M610082200· OSTI ID:909759

Rigby, K; Zhang, L; Cobine, P A; George, G N; Winge, D R

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 CX{sub 9}C 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.

• Research Organization: Stanford Linear Accelerator Center (SLAC)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC02-76SF00515
• OSTI ID: 909759
• Report Number(s): SLAC-REPRINT-2007-131
• Journal Information: J.Biol.Chem.282:10233-10242,2007, Journal Name: J.Biol.Chem.282:10233-10242,2007 Vol. 282; ISSN JBCHA3; ISSN 0021-9258
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
COPPER
CYTOCHROMES
FUNCTIONALS
IN VIVO
MONOMERS
OXIDASES
Other
OTHER
PROTEINS
RESIDUES
SACCHAROMYCES
TRANSIENTS