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Archaea
Volume 2013 (2013), Article ID 920241, 7 pages
http://dx.doi.org/10.1155/2013/920241
Research Article

Localization of Methyl-Coenzyme M Reductase as Metabolic Marker for Diverse Methanogenic Archaea

1Institute of Microbiology and Genetics, Georg-August-Universität Göttingen, Grisebachstraße 8, 37077 Göttingen, Germany
2Hannover Medical School, Institute of Functional and Applied Anatomy, Carl-Neuberg-Straße 1, 30625 Hannover, Germany
3Behavioral Ecology and Sociobiology Unit, German Primate Center, Kellnerweg 4, 37077 Göttingen, Germany
4School of Veterinary and Biomedical Sciences, Murdoch University, 90 South Street Murdoch, WA 6150, Australia
5Courant Centre Geobiology, Georg-August-Universität Göttingen, Goldschmidtstraße 3, 37077 Göttingen, Germany

Received 21 September 2012; Accepted 9 January 2013

Academic Editor: J. Reitner

Copyright © 2013 Christoph Wrede et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Methyl-Coenzyme M reductase (MCR) as key enzyme for methanogenesis as well as for anaerobic oxidation of methane represents an important metabolic marker for both processes in microbial biofilms. Here, the potential of MCR-specific polyclonal antibodies as metabolic marker in various methanogenic Archaea is shown. For standard growth conditions in laboratory culture, the cytoplasmic localization of the enzyme in Methanothermobacter marburgensis, Methanothermobacter wolfei, Methanococcus maripaludis, Methanosarcina mazei, and in anaerobically methane-oxidizing biofilms is demonstrated. Under growth limiting conditions on nickel-depleted media, at low linear growth of cultures, a fraction of 50–70% of the enzyme was localized close to the cytoplasmic membrane, which implies “facultative” membrane association of the enzyme. This feature may be also useful for assessment of growth-limiting conditions in microbial biofilms.