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  Thermophilic archaea activate butane via alkyl-coenzyme M formation.

Laso-Pérez, R., Wegener, G., Knittel, K., Widdel, F., Harding, K. J., Krukenberg, V., et al. (2016). Thermophilic archaea activate butane via alkyl-coenzyme M formation. Nature, 539(7629), 396-401. doi:10.1038/nature20152.

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Laso-Pérez, R., Author
Wegener, G., Author
Knittel, K., Author
Widdel, F., Author
Harding, K. J., Author
Krukenberg, V., Author
Meier, D. V., Author
Richter, M., Author
Tegetmeyer, H. E., Author
Riedel, D.1, Author           
Richnow, H. H., Author
Adrian, L., Author
Reemtsma, T., Author
Lechtenfeld, O. J., Author
Musat, F., Author
Affiliations:
1Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              

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Free keywords: Archaeal physiology; Metabolomics; Environmental microbiology
 Abstract: The anaerobic formation and oxidation of methane involve unique enzymatic mechanisms and cofactors, all of which are believed to be specific for C1-compounds. Here we show that an anaerobic thermophilic enrichment culture composed of dense consortia of archaea and bacteria apparently uses partly similar pathways to oxidize the C4 hydrocarbon butane. The archaea, proposed genus ‘Candidatus Syntrophoarchaeum’, show the characteristic autofluorescence of methanogens, and contain highly expressed genes encoding enzymes similar to methyl-coenzyme M reductase. We detect butyl-coenzyme M, indicating archaeal butane activation analogous to the first step in anaerobic methane oxidation. In addition, Ca. Syntrophoarchaeum expresses the genes encoding β-oxidation enzymes, carbon monoxide dehydrogenase and reversible C1 methanogenesis enzymes. This allows for the complete oxidation of butane. Reducing equivalents are seemingly channelled to HotSeep-1, a thermophilic sulfate-reducing partner bacterium known from the anaerobic oxidation of methane. Genes encoding 16S rRNA and methyl-coenzyme M reductase similar to those identifying Ca. Syntrophoarchaeum were repeatedly retrieved from marine subsurface sediments, suggesting that the presented activation mechanism is naturally widespread in the anaerobic oxidation of short-chain hydrocarbons.

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Language(s): eng - English
 Dates: 2016-10-172016-11-17
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/nature20152
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Title: Nature
Source Genre: Journal
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Pages: - Volume / Issue: 539 (7629) Sequence Number: - Start / End Page: 396 - 401 Identifier: -