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  A conspicuous nickel protein in microbial mats that oxidize methane anaerobically

Krüger, M., Meyerdierks, A., Glöckner, F. O., Amann, R., Widdel, F., Kube, M., et al. (2003). A conspicuous nickel protein in microbial mats that oxidize methane anaerobically. Nature, 426(6968), 878-881. doi:10.1038/nature02207.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-894C-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-894D-E
Genre: Journal Article
Alternative Title : Nature

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 Creators:
Krüger, Martin, Author
Meyerdierks, Anke, Author
Glöckner, Frank Oliver, Author
Amann, Rudolf, Author
Widdel, Friedrich, Author
Kube, Michael1, Author              
Reinhardt, Richard1, Author              
Kahnt, Jörg, Author
Böcher, Reinhard, Author
Thauer, Rudolf K., Author
Shima, Seigo, Author
Affiliations:
1High Throughput Technologies, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433552              

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 Abstract: Anaerobic oxidation of methane (AOM) in marine sediments is an important microbial process in the global carbon cycle and in control of greenhouse gas emission. The responsible organisms supposedly reverse the reactions of methanogenesis1-8, but cultures providing biochemical proof of this have not been isolated. Here we searched for AOM-associated cell components in microbial mats from anoxic methane seeps in the Black Sea9-11. These mats catalyse AOM rather than carry out methanogenesis. We extracted a prominent nickel compound displaying the same absorption spectrum as the nickel cofactor F430 of methyl-coenzyme M reductase, the terminal enzyme of methanogenesis12; however, the nickel compound exhibited a higher molecular mass than F430. The apparent variant of F430 was part of an abundant protein that was purified from the mat and that consists of three different subunits. Determined amino-terminal amino acid sequences matched a gene locus cloned from the mat. Sequence analyses revealed similarities to methyl-coenzyme M reductase from methanogenic archaea. The abundance of the nickel protein (7% of extracted proteins) in the mat suggests an important role in AOM.

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Language(s): eng - English
 Dates: 2003-12-18
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: -
 Identifiers: eDoc: 173938
ISI: 000187342000068
DOI: 10.1038/nature02207
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Title: Nature
  Alternative Title : Nature
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 426 (6968) Sequence Number: - Start / End Page: 878 - 881 Identifier: ISSN: 0028-0836