This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bäcklund, A. S.
Right arrow Articles by Nilsson, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bäcklund, A. S.
Right arrow Articles by Nilsson, T.
Agricola
Right arrow Articles by Bäcklund, A. S.
Right arrow Articles by Nilsson, T.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, April 2009, p. 2439-2445, Vol. 75, No. 8
0099-2240/09/$08.00+0     doi:10.1128/AEM.01325-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Periplasmic c Cytochromes and Chlorate Reduction in Ideonella dechloratans{triangledown}

Anna Smedja Bäcklund,1 Jan Bohlin,1 Niklas Gustavsson,2,§ and Thomas Nilsson1*

Department of Chemistry and Biomedical Sciences, Faculty of Technology and Science, Karlstad University, SE-651 88 Karlstad, Sweden,1 Department of Biochemistry, Lund University, SE-221 00 Lund, Sweden2

Received 13 June 2008/ Accepted 11 February 2009

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.

* Corresponding author. Mailing address: Department of Chemistry and Biomedical Sciences, Faculty of Technology and Science, Karlstad University, SE-651 88 Karlstad, Sweden. Phone: 46-54-7001776. Fax: 46-54-7001457. E-mail: thomas.nilsson{at}kau.se

{triangledown} Published ahead of print on 20 February 2009.

§ Present address: Novozymes Biopharma AB, SE-220 09 Lund, Sweden.

Applied and Environmental Microbiology, April 2009, p. 2439-2445, Vol. 75, No. 8
0099-2240/09/$08.00+0     doi:10.1128/AEM.01325-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Branco, R., Francisco, R., Chung, A. P., Morais, P. V. (2009). Identification of an aox System That Requires Cytochrome c in the Highly Arsenic-Resistant Bacterium Ochrobactrum tritici SCII24. Appl. Environ. Microbiol. 75: 5141-5147 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»