Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Characterization of a candidate cytochome c gene associated with the gene cluster for chlorate respiration in Ideonella dechloratans
Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
Novozymes Biopharma AB, Lund, Sweden.
Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
Show others and affiliations
(English)Manuscript (Other (popular science, discussion, etc.))
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:kau:diva-3828OAI: oai:DiVA.org:kau-3828DiVA: diva2:208845
Available from: 2009-03-20 Created: 2009-03-20 Last updated: 2011-10-18Bibliographically approved
In thesis
1. Electron transport in microbial chlorate respiration
Open this publication in new window or tab >>Electron transport in microbial chlorate respiration
2009 (English)Licentiate thesis, comprehensive summary (Other academic)
Abstract [en]

Several bacterial species are capable to use perchlorate and/or chlorate as an alternative electron acceptor in absence of oxygen. Microbial respiration of oxochlorates is important for biotreatment of effluent from industries where oxochlorates are produced or handled. One of these species, the Gram-negative Ideonella dechloratans, is able to reduce chlorate but not perchlorate. Two soluble enzymes, chlorate reductase and chlorite dismutase, participate in the conversion of chlorate into chloride and molecular oxygen. The present study deals with the electron transport from the membrane-bound components to the periplasmic chlorate reductase. Soluble c cytochromes were investigated for their ability to serve as electron donors to chlorate reductase. The results show that a 6 kDa c cytochrome serves as electron donor for chlorate reductase. This cytochrome also serves as electron donor for a terminal oxidase in the reduction of oxygen that is produced in the course of chlorate respiration. A gene encoding a soluble c cytochrome was found in close proximity to the gene cluster for chlorate reduction. This gene was cloned and expressed heterologously, and the resulting protein was investigated as a candidate electron donor for chlorate reductase. Electron transfer from this protein could not be demonstrated, suggesting that the gene product does not serve as immediate electron donor for chlorate reductase.

 

Place, publisher, year, edition, pages
Karlstad: Karlstad University, 2009. 24 p.
Series
Karlstad University Studies, ISSN 1403-8099 ; 2009:18
Keyword
c cytochromes, chlorate reduction, electron transport, c cytokromer, kloratreduktion, elektrontransport
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Research subject
Chemistry
Identifiers
urn:nbn:se:kau:diva-3777 (URN)978-91-7063-241-9 (ISBN)
Presentation
2009-04-17, Ericssonsalen, 9C 204, Karlstads universitet, Karlstad, 13:15 (English)
Opponent
Supervisors
Available from: 2009-03-20 Created: 2009-03-09 Last updated: 2011-11-14Bibliographically approved

Open Access in DiVA

No full text

Search in DiVA

By author/editor
Bohlin, JanSmedja Bäcklund, AnnaWahlberg, SaraNilsson, Thomas
By organisation
Department of Chemistry and Biomedical Sciences
Chemical Sciences

Search outside of DiVA

GoogleGoogle Scholar

Total: 59 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf