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  Thermophilic archaea activate butan via alkyl-coenzyme M formation

Laso-Perez, R., Wegener, G., Knittel, K., Widdel, F., Harding, K. J., Krukenberg, V., et al. (2016). Thermophilic archaea activate butan via alkyl-coenzyme M formation. Nature, 539: 1, pp. 396-401.

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Laso-Perez, Rafael1, Author
Wegener, Gunter2, Author           
Knittel, Katrin3, Author           
Widdel, Friedrich4, Author           
Harding, Katie Jean5, Author           
Krukenberg, Viola2, Author           
Meier, Dimitri3, Author           
Richter, Michael6, Author           
Tegetmeyer, Halina E.2, Author           
Riedel, Dietmar, Author
Richnow, Hans-Hermann, Author
Adrian, Lorenz, Author
Reemtsma, Thorsten, Author
Lechtenfeld, Oliver J., Author
Musat, Florin4, Author           
Affiliations:
1Max Planck Society, ou_persistent13              
2HGF MPG Joint Research Group for Deep Sea Ecology & Technology, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481702              
3Department of Molecular Ecology, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481696              
4Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481695              
5Department of Biogeochemistry, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481693              
6Microbial Genomics Group, Department of Molecular Ecology, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481697              

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 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: 2016-11-17
 Publication Status: Issued
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 Rev. Type: Internal
 Identifiers: eDoc: 733274
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Title: Nature
Source Genre: Journal
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Pages: - Volume / Issue: 539 Sequence Number: 1 Start / End Page: 396 - 401 Identifier: -