PMID- 10617659
OWN - NLM
STAT- MEDLINE
DCOM- 20000131
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 1
DP  - 2000 Jan 7
TI  - Cox11p is required for stable formation of the Cu(B) and magnesium centers of
      cytochrome c oxidase.
PG  - 619-23
AB  - Assembly of the core subunits of the aa(3)-type cytochrome c oxidase in
      mitochondria and aerobic bacteria such as Rhodobacter sphaeroides requires the
      association of three subunits and the formation of five to seven metal centers.
      Several assembly proteins are required for the late stages of oxidase assembly in
      eukaryotes; some of these are also present in Rb. sphaeroides. To investigate the
      role of one of these proteins, Cox11p, the mitochondrial-like oxidase of Rb.
      sphaeroides was overexpressed and purified from cells that lacked cox11, the gene
      for Cox11p. The oxidase that assembled in the absence of Cox11p lacked Cu(B) at
      the active site and contained greatly reduced amounts of metal at the
      magnesium/manganese-binding site between subunits I and II. This inactive
      oxidase, however, did contain hemes a and a(3), Cu(A), and all three subunits.
      These results indicate that Cox11p is required at a late, perhaps final, step in 
      the assembly of cytochrome oxidase, most likely the insertion of Cu(B). Oxidase
      which assembled in a strain with a low copy number of cox11 appeared nearly wild 
      type, suggesting that Cox11p is required in substoichiometric amounts for its
      role in oxidase assembly.
FAU - Hiser, L
AU  - Hiser L
AD  - Department of Biochemistry, University of Mississippi Medical Center, Jackson,
      Mississippi 39216, USA.
FAU - Di Valentin, M
AU  - Di Valentin M
FAU - Hamer, A G
AU  - Hamer AG
FAU - Hosler, J P
AU  - Hosler JP
LA  - eng
GR  - GM25480/GM/NIGMS NIH HHS/United States
GR  - GM56824/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (COX11 protein, S cerevisiae)
RN  - 0 (Membrane Proteins)
RN  - 0 (Mitochondrial Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 42VZT0U6YR (Heme)
RN  - 42Z2K6ZL8P (Manganese)
RN  - 789U1901C5 (Copper)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - I38ZP9992A (Magnesium)
SB  - IM
MH  - Catalytic Domain
MH  - Copper/analysis/*metabolism
MH  - Electron Spin Resonance Spectroscopy
MH  - Electron Transport Complex IV/*biosynthesis/chemistry/genetics
MH  - Heme/analysis
MH  - Magnesium/analysis/*metabolism
MH  - Manganese/analysis
MH  - Membrane Proteins/analysis/*metabolism
MH  - Mitochondrial Proteins
MH  - Oxidation-Reduction
MH  - Oxygen Consumption
MH  - Recombinant Proteins/metabolism
MH  - Rhodobacter sphaeroides/*enzymology
MH  - *Saccharomyces cerevisiae Proteins
MH  - Spectrophotometry
EDAT- 2000/01/05 00:00
MHDA- 2000/01/05 00:01
CRDT- 2000/01/05 00:00
PHST- 2000/01/05 00:00 [pubmed]
PHST- 2000/01/05 00:01 [medline]
PHST- 2000/01/05 00:00 [entrez]
AID - 10.1074/jbc.275.1.619 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 Jan 7;275(1):619-23. doi: 10.1074/jbc.275.1.619.