PMID- 23103386
OWN - NLM
STAT- MEDLINE
DCOM- 20130408
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1827
IP  - 3
DP  - 2013 Mar
TI  - True wild type and recombinant wild type cytochrome c oxidase from Paracoccus 
      denitrificans show a 20-fold difference in their catalase activity.
PG  - 319-27
LID - S0005-2728(12)01056-0 [pii]
LID - 10.1016/j.bbabio.2012.10.008 [doi]
AB  - The four subunit (SU) aa(3) cytochrome c oxidase (CcO) from Paracoccus 
      denitrificans is one of the terminal enzymes of the respiratory chain. Its 
      binuclear active center, residing in SU I, contains heme a(3) and Cu(B). Apart 
      from its oxygen reductase activity, the protein possesses a peroxidase and a 
      catalase activity. To compare variants and the wild type (WT) protein in a more 
      stringent way, a recombinant (rec.) WT strain was constructed, carrying the gene 
      for SU I on a low copy number plasmid. This rec. WT showed no difference in 
      oxygen reductase activity compared to the American Type Culture Collection (ATCC) 
      WT CcO but surprisingly its catalase activity was increased by a factor of 20. 
      The potential over-production of SU I might impair the correct insertion of heme 
      a(3) and Cu(B) because of a deficiency in metal inserting chaperones. An altered 
      distance between heme a(3) and Cu(B) and variations in protein structure are 
      possible reasons for the observed increased catalase activity. The availability 
      of chaperones was improved by cloning the genes ctaG and surf1c on the same 
      plasmid as the SU I gene. The new rec. WT CcO showed in fact a reduced catalase 
      activity. Using differential scanning calorimetry no significant difference in 
      thermal stability between the ATCC WT CcO and the rec. WT CcO was detected. 
      However, upon aging the thermal stability of the rec. WT CcO was reduced compared 
      to that of the ATCC WT CcO pointing to a decreased structural stability of the 
      rec. WT CcO.
CI  - Copyright (c) 2012 Elsevier B.V. All rights reserved.
FAU - Hilbers, Florian
AU  - Hilbers F
AD  - Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt am 
      Main, Germany. Florian.Hilbers@biophys.mpg.de
FAU - von der Hocht, Iris
AU  - von der Hocht I
FAU - Ludwig, Bernd
AU  - Ludwig B
FAU - Michel, Hartmut
AU  - Michel H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20121024
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Recombinant Proteins)
RN  - EC 1.11.1.6 (Catalase)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Calorimetry, Differential Scanning
MH  - Catalase/*metabolism
MH  - Cloning, Molecular
MH  - Electron Transport Complex IV/*metabolism
MH  - Kinetics
MH  - Paracoccus denitrificans/*enzymology
MH  - Recombinant Proteins/metabolism
EDAT- 2012/10/30 06:00
MHDA- 2013/04/09 06:00
CRDT- 2012/10/30 06:00
PHST- 2012/07/17 00:00 [received]
PHST- 2012/10/15 00:00 [revised]
PHST- 2012/10/18 00:00 [accepted]
PHST- 2012/10/30 06:00 [entrez]
PHST- 2012/10/30 06:00 [pubmed]
PHST- 2013/04/09 06:00 [medline]
AID - S0005-2728(12)01056-0 [pii]
AID - 10.1016/j.bbabio.2012.10.008 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2013 Mar;1827(3):319-27. doi: 10.1016/j.bbabio.2012.10.008. 
      Epub 2012 Oct 24.