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Periplasmic c Cytochromes and Chlorate Reduction 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.
Department of Biochemistry, Lund University.
Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
2009 (English)In: Applied and Environmental Microbiology, ISSN 0099-2240, E-ISSN 1098-5336, Vol. 75, p. 2439-2445Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2009. Vol. 75, p. 2439-2445
National Category
Biochemistry and Molecular Biology
Research subject
Chemistry
Identifiers
URN: urn:nbn:se:kau:diva-2804DOI: 10.1128/AEM.01325-08OAI: oai:DiVA.org:kau-2804DiVA, id: diva2:37584
Note

Artikelns titel i Anna Smedja Bäcklunds licentiatuppsats (2009): "Periplasmic c cytochromes coupled to chlorate reduction in Ideonella dechloratans" Artikelns titel i Jan Bohlins doktorsavhandling (2008): "Periplasmic c cytochromes coupled to chlorate reduction in Ideonella dechloratans"

Available from: 2008-10-08 Created: 2008-10-08 Last updated: 2018-01-23Bibliographically approved
In thesis
1. Enzymes and electron transport in microbial chlorate respiration
Open this publication in new window or tab >>Enzymes and electron transport in microbial chlorate respiration
2008 (English)Doctoral thesis, comprehensive summary (Other scientific)
Abstract [en]

Microbial chlorate respiration plays an important role in the turnover of oxochlorates in nature and industrial waste management. This thesis deals with the characterization of the molecular components of chlorate respiration in Ideonella dechloratans. Chlorate respiration utilizes two soluble periplasmic enzymes, chlorate reductase and chlorite dismutase, to convert chlorate to chloride and oxygen. The genes encoding the enzymes participating in the chlorate degradation have been sequenced, and are found in close proximity, forming a gene cluster for chlorate metabolism. This work also includes the successful recombinant expression of three genes from Ideonella dechloratans. Two of the gene products, chlorite dismutase and the C subunit of chlorate reductase, participate in the chlorate respiration. The third gene, which is found close to the gene cluster for chlorate metabolism, encodes a soluble c-type cytochrome. The localization of the gene suggests the corresponding protein as a candidate for a role as electron donor to chlorate reductase. Also, the role of soluble periplasmic c cytochromes of Ideonella dechloratans in chlorate respiration was studied. At least one of the soluble c cytochromes was found capable of serving as electron donor for chlorate reduction. This c cytochrome, and several others, can also donate electrons to a terminal oxidase for subsequent reduction of oxygen, as required for the branched electron flow during chlorate respiration.

Place, publisher, year, edition, pages
Karlstad: Karlstad University, 2008. p. 36
Series
Karlstad University Studies, ISSN 1403-8099 ; 2008:36
Keywords
Ideonella dechloratans, c cytochromes, chlorate, chlorate reductase, chlorite dismutase, heterologous expression, heme reconstitution, electron transport, oxidoreductas
National Category
Chemical Sciences
Research subject
Chemistry
Identifiers
urn:nbn:se:kau:diva-2805 (URN)978-91-7063-196-2 (ISBN)
Public defence
2008-10-17, 9C 204, Ericssonsalen, Karlstads universitet, Karlstad, 10:30 (Swedish)
Opponent
Supervisors
Available from: 2008-10-13 Created: 2008-10-08 Last updated: 2018-01-23Bibliographically approved
2. 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. p. 24
Series
Karlstad University Studies, ISSN 1403-8099 ; 2009:18
Keywords
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
3. c Cytochromes as Electron Carriers in Microbial Chlorate Respiration
Open this publication in new window or tab >>c Cytochromes as Electron Carriers in Microbial Chlorate Respiration
2011 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Microbial respiration of oxochlorates is important for the biotreatment of effluents from industries where oxochlorates are produced or handled. Several bacterial species are capable to use perchlorate and/or chlorate as an alternative electron acceptor in absence of oxygen. The present study deals with the electron transport from the membrane-bound components to the periplasmic chlorate reductase, in the gram-negative bacterium Ideonella dechloratans. Both chlorate reductase and the terminal oxidase of I. dechloratans were found to utilize soluble c cytochromes as electron donors. For further investigation, two major heme-containing components were purified and characterized. The most abundant was a 9 kDa c-type cytochrome (class I), denoted cytochrome c-Id1. This protein was shown to serve as electron donor for both chlorate reductase, and for a terminal oxidase. The other major component was a 55 kDa homotetrameric cytochrome c', (class II). A function for this cytochrome could not be demonstrated but it does not appear to serve as electron donor to chlorate reductase. A gene predicted to encode a soluble c cytochrome was found in close proximity to the gene cluster for chlorate reduction. The predicted sequence did not match any of the cytochromes discussed above. The 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, 2011. p. 48
Series
Karlstad University Studies, ISSN 1403-8099 ; 2011:40
Keywords
c cytochrome, chlorate reduction, electron transport
National Category
Biochemistry and Molecular Biology
Research subject
Chemistry
Identifiers
urn:nbn:se:kau:diva-8038 (URN)978-91-7063-375-1 (ISBN)
Public defence
2011-09-30, Andersalen, 11D 121, Karlstads universitet, Karlstad, 10:15 (Swedish)
Opponent
Supervisors
Available from: 2011-09-06 Created: 2011-08-11 Last updated: 2011-11-14Bibliographically approved

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Smedja Bäcklund, AnnaBohlin, JanNilsson, Thomas

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