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 Shima, S.
Right arrow Articles by Thauer, R. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shima, S.
Right arrow Articles by Thauer, R. K.
Agricola
Right arrow Articles by Shima, S.
Right arrow Articles by Thauer, R. K.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, July 2001, p. 3041-3045, Vol. 67, No. 7
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.7.3041-3045.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Characterization of a Heme-Dependent Catalase from Methanobrevibacter arboriphilus†

Seigo Shima,1,* Melanie Sordel-Klippert,1 Andrei Brioukhanov,2 Alexander Netrusov,2 Dietmar Linder,3 and Rudolf K. Thauer1

Max-Planck-Institut für Terrestrische Mikrobiologie and Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität, D-35043 Marburg,1 and Biochemisches Institut, Fachbereich Humanmedizin, Justus-Liebig-Universität, D-35392 Gießen,3 Germany, and Microbiology Department, Moscow Lomonosov State University, Moscow 119899, Russia2

Received 2 February 2001/Accepted 3 May 2001

Recently it was reported that methanogens of the genus Methanobrevibacter exhibit catalase activity. This was surprising, since Methanobrevibacter species belong to the order Methanobacteriales, which are known not to contain cytochromes and to lack the ability to synthesize heme. We report here that Methanobrevibacter arboriphilus strains AZ and DH1 contained catalase activity only when the growth medium was supplemented with hemin. The heme catalase was purified and characterized, and the encoding gene was cloned. The amino acid sequence of the catalase from the methanogens is most similar to that of Methanosarcina barkeri.


* Corresponding author. Mailing address: Max-Planck-Institut für terrestrische Mikrobiologie, Karl-von-Frisch-Strasse, D-35043 Marburg, Germany. Phone: (49) 6421-178200. Fax: (49) 6421-178209. E-mail: shima{at}mailer.uni-marburg.de.

dagger Dedicated to Hans Trüper on the occasion of his 65th birthday.


Applied and Environmental Microbiology, July 2001, p. 3041-3045, Vol. 67, No. 7
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.7.3041-3045.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Brioukhanov, A. L., Netrusov, A. I., Eggen, R. I. L. (2006). The catalase and superoxide dismutase genes are transcriptionally up-regulated upon oxidative stress in the strictly anaerobic archaeon Methanosarcina barkeri. Microbiology 152: 1671-1677 [Abstract] [Full Text]  
  • Fricke, W. F., Seedorf, H., Henne, A., Kruer, M., Liesegang, H., Hedderich, R., Gottschalk, G., Thauer, R. K. (2006). The Genome Sequence of Methanosphaera stadtmanae Reveals Why This Human Intestinal Archaeon Is Restricted to Methanol and H2 for Methane Formation and ATP Synthesis. J. Bacteriol. 188: 642-658 [Abstract] [Full Text]  
  • Boga, H. I., Brune, A. (2003). Hydrogen-Dependent Oxygen Reduction by Homoacetogenic Bacteria Isolated from Termite Guts. Appl. Environ. Microbiol. 69: 779-786 [Abstract] [Full Text]  
  • Amo, T., Atomi, H., Imanaka, T. (2002). Unique Presence of a Manganese Catalase in a Hyperthermophilic Archaeon, Pyrobaculum calidifontis VA1. J. Bacteriol. 184: 3305-3312 [Abstract] [Full Text]