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Periplasmic c Cytochromes and Chlorate Reduction in Ideonella dechloratans

Backlund, Anna Smedja; Bohlin, Jan; Gustavsson, Niklas LU and Nilsson, Thomas (2009) In Applied and Environmental Microbiology 75(8). p.2439-2445
Abstract
The aim of this study was to clarify the pathway of electron transfer between the inner membrane components and the periplasmic chlorate reductase. Several soluble c-type cytochromes were found in the periplasm. The optical difference spectrum of dithionite-reduced periplasmic extract shows that at least one of these components is capable of acting as an electron donor to the enzyme chlorate reductase. The cytochromes were partially separated, and the fractions were analyzed by UV/visible spectroscopy to determine the ability of donating electrons to chlorate reductase. Our results show that one of the c cytochromes (6 kDa) is able to donate electrons, both to chlorate reductase and to the membrane-bound cytochrome c oxidase, whereas the... (More)
The aim of this study was to clarify the pathway of electron transfer between the inner membrane components and the periplasmic chlorate reductase. Several soluble c-type cytochromes were found in the periplasm. The optical difference spectrum of dithionite-reduced periplasmic extract shows that at least one of these components is capable of acting as an electron donor to the enzyme chlorate reductase. The cytochromes were partially separated, and the fractions were analyzed by UV/visible spectroscopy to determine the ability of donating electrons to chlorate reductase. Our results show that one of the c cytochromes (6 kDa) is able to donate electrons, both to chlorate reductase and to the membrane-bound cytochrome c oxidase, whereas the roles of the remaining c cytochromes still remain to be elucidated. Peptide extracts of the c cytochromes were obtained by tryptic in-gel digestion for matrix-assisted laser desorption ionization -time of flight mass spectrometry analysis. Peptide sequences obtained indicate that the 6-kDa cytochrome c protein is similar to c cytochromes from the chlorate-reducing bacterium Dechloromonas aromatica. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Applied and Environmental Microbiology
volume
75
issue
8
pages
2439 - 2445
publisher
American Society for Microbiology
external identifiers
  • wos:000264936800024
  • pmid:19233956
  • scopus:64749109757
ISSN
0099-2240
DOI
10.1128/AEM.01325-08
language
English
LU publication?
yes
id
0e4656d0-ee6d-4530-be21-b61a51e388cd (old id 1400783)
date added to LUP
2009-06-12 10:16:23
date last changed
2017-01-01 04:44:20
@article{0e4656d0-ee6d-4530-be21-b61a51e388cd,
  abstract     = {The aim of this study was to clarify the pathway of electron transfer between the inner membrane components and the periplasmic chlorate reductase. Several soluble c-type cytochromes were found in the periplasm. The optical difference spectrum of dithionite-reduced periplasmic extract shows that at least one of these components is capable of acting as an electron donor to the enzyme chlorate reductase. The cytochromes were partially separated, and the fractions were analyzed by UV/visible spectroscopy to determine the ability of donating electrons to chlorate reductase. Our results show that one of the c cytochromes (6 kDa) is able to donate electrons, both to chlorate reductase and to the membrane-bound cytochrome c oxidase, whereas the roles of the remaining c cytochromes still remain to be elucidated. Peptide extracts of the c cytochromes were obtained by tryptic in-gel digestion for matrix-assisted laser desorption ionization -time of flight mass spectrometry analysis. Peptide sequences obtained indicate that the 6-kDa cytochrome c protein is similar to c cytochromes from the chlorate-reducing bacterium Dechloromonas aromatica.},
  author       = {Backlund, Anna Smedja and Bohlin, Jan and Gustavsson, Niklas and Nilsson, Thomas},
  issn         = {0099-2240},
  language     = {eng},
  number       = {8},
  pages        = {2439--2445},
  publisher    = {American Society for Microbiology},
  series       = {Applied and Environmental Microbiology},
  title        = {Periplasmic c Cytochromes and Chlorate Reduction in Ideonella dechloratans},
  url          = {http://dx.doi.org/10.1128/AEM.01325-08},
  volume       = {75},
  year         = {2009},
}