PMID- 20442397
OWN - NLM
STAT- MEDLINE
DCOM- 20100812
LR  - 20231105
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 285
IP  - 28
DP  - 2010 Jul 9
TI  - An unconventional copper protein required for cytochrome c oxidase respiratory 
      function under extreme acidic conditions.
PG  - 21519-25
LID - 10.1074/jbc.M110.131359 [doi]
AB  - Very little is known about the processes used by acidophile organisms to preserve 
      stability and function of respiratory pathways. Here, we reveal a potential 
      strategy of these organisms for protecting and keeping functional key enzymes 
      under extreme conditions. Using Acidithiobacillus ferrooxidans, we have 
      identified a protein belonging to a new cupredoxin subfamily, AcoP, for 
      "acidophile CcO partner," which is required for the cytochrome c oxidase (CcO) 
      function. We show that it is a multifunctional copper protein with at least two 
      roles as follows: (i) as a chaperone-like protein involved in the protection of 
      the Cu(A) center of the CcO complex and (ii) as a linker between the periplasmic 
      cytochrome c and the inner membrane cytochrome c oxidase. It could represent an 
      interesting model for investigating the multifunctionality of proteins known to 
      be crucial in pathways of energy metabolism.
FAU - Castelle, Cindy
AU  - Castelle C
AD  - Laboratoire de Bioenergetique et Ingenierie des Proteines, IMM-CNRS, 13402 
      Marseille Cedex 20, France.
FAU - Ilbert, Marianne
AU  - Ilbert M
FAU - Infossi, Pascale
AU  - Infossi P
FAU - Leroy, Gisele
AU  - Leroy G
FAU - Giudici-Orticoni, Marie-Therese
AU  - Giudici-Orticoni MT
LA  - eng
PT  - Journal Article
DEP - 20100503
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Metalloproteins)
RN  - 0 (cupredoxin)
RN  - 12284-43-4 (Azurin)
RN  - 789U1901C5 (Copper)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Acidithiobacillus/*enzymology
MH  - Azurin/chemistry
MH  - Copper/chemistry
MH  - Electron Spin Resonance Spectroscopy
MH  - Electron Transport Complex IV/*metabolism
MH  - Electrophoresis
MH  - Hydrogen-Ion Concentration
MH  - Mass Spectrometry/methods
MH  - Metalloproteins/chemistry/genetics
MH  - Models, Biological
MH  - Oxidation-Reduction
MH  - Oxygen Consumption
MH  - Protein Binding
MH  - Surface Plasmon Resonance
MH  - Time Factors
PMC - PMC2898452
EDAT- 2010/05/06 06:00
MHDA- 2010/08/13 06:00
PMCR- 2011/07/09
CRDT- 2010/05/06 06:00
PHST- 2010/05/06 06:00 [entrez]
PHST- 2010/05/06 06:00 [pubmed]
PHST- 2010/08/13 06:00 [medline]
PHST- 2011/07/09 00:00 [pmc-release]
AID - S0021-9258(20)60179-X [pii]
AID - M110.131359 [pii]
AID - 10.1074/jbc.M110.131359 [doi]
PST - ppublish
SO  - J Biol Chem. 2010 Jul 9;285(28):21519-25. doi: 10.1074/jbc.M110.131359. Epub 2010 
      May 3.