PMID- 18055590
OWN - NLM
STAT- MEDLINE
DCOM- 20080212
LR  - 20211020
IS  - 1098-5530 (Electronic)
IS  - 0021-9193 (Print)
IS  - 0021-9193 (Linking)
VI  - 190
IP  - 3
DP  - 2008 Feb
TI  - Identification of two catalases in Azotobacter vinelandii: a KatG homologue and a 
      novel bacterial cytochrome c catalase, CCCAv.
PG  - 954-62
AB  - Azotobacter vinelandii produces two detectable catalases during growth on minimal 
      medium. The heat-labile catalase expressed during exponential growth phase was 
      identified as a KatG homologue by liquid chromatography-tandem mass spectrometry 
      (LC-MS/MS) using a mixed protein sample. The second catalase was heat resistant 
      and had substantial residual activity after treatment at 90 degrees C. This 
      enzyme was purified by anion-exchange and size exclusion chromatography and was 
      found to exhibit strong absorption at 407 nm, which is often indicative of 
      associated heme moieties. The purified protein was fragmented by proteinase K and 
      identified by LC-MS/MS. Some identity was shared with the MauG/bacterial 
      cytochrome c peroxidase (BCCP) protein family, but the enzyme exhibited a strong 
      catalase activity never before observed in this family. Because two putative 
      c-type heme sites (CXXCH) were predicted in the peptide sequence and were 
      demonstrated experimentally, the enzyme was designated a cytochrome c catalase 
      (CCC(Av)). However, the local organization of the CCC(Av) heme motifs differed 
      significantly from that of the BCCPs as the sites were confined to the C-terminal 
      half of the catalase. A possible Ca2+ binding motif, previously described in the 
      BCCPs, is also present in the CCC(Av) peptide sequence. Some instability in the 
      presence of EGTA was observed. Expression of the catalase was abolished in cccA 
      mutants, resulting in a nearly 8,700-fold reduction in peroxide resistance in 
      stationary phase.
FAU - Sandercock, James R
AU  - Sandercock JR
AD  - Department of Biological Sciences, University of Alberta, Edmonton, Alberta, 
      Canada T6G2E9.
FAU - Page, William J
AU  - Page WJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20071130
PL  - United States
TA  - J Bacteriol
JT  - Journal of bacteriology
JID - 2985120R
RN  - 0 (Bacterial Proteins)
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Sigma Factor)
RN  - 0 (sigma factor KatF protein, Bacteria)
RN  - 9007-43-6 (Cytochromes c)
RN  - BBX060AN9V (Hydrogen Peroxide)
RN  - EC 1.11.1.6 (Catalase)
RN  - EC 1.11.1.6 (katG protein, E coli)
SB  - IM
MH  - Amino Acid Sequence
MH  - Azotobacter vinelandii/drug effects/*enzymology/growth & development/*physiology
MH  - Bacterial Proteins/genetics/metabolism
MH  - Catalase/chemistry/*genetics/isolation & purification/metabolism
MH  - Chromatography, Liquid
MH  - *Cytochromes c/chemistry/genetics/isolation & purification/metabolism
MH  - Enzyme Stability
MH  - Escherichia coli Proteins/chemistry/*genetics/metabolism
MH  - Hot Temperature
MH  - Hydrogen Peroxide/pharmacology
MH  - Molecular Sequence Data
MH  - Sequence Alignment
MH  - *Sequence Homology, Amino Acid
MH  - Sigma Factor/metabolism
MH  - Tandem Mass Spectrometry
PMC - PMC2223588
EDAT- 2007/12/07 09:00
MHDA- 2008/02/13 09:00
PMCR- 2008/06/01
CRDT- 2007/12/07 09:00
PHST- 2007/12/07 09:00 [pubmed]
PHST- 2008/02/13 09:00 [medline]
PHST- 2007/12/07 09:00 [entrez]
PHST- 2008/06/01 00:00 [pmc-release]
AID - JB.01572-06 [pii]
AID - 1572-06 [pii]
AID - 10.1128/JB.01572-06 [doi]
PST - ppublish
SO  - J Bacteriol. 2008 Feb;190(3):954-62. doi: 10.1128/JB.01572-06. Epub 2007 Nov 30.