Thermophilic archaea activate butane via alkyl-coenzyme M formation

Rafael Laso-Pérez, Gunter Wegener (), Katrin Knittel, Friedrich Widdel, Katie J. Harding, Viola Krukenberg, Dimitri V. Meier, Michael Richter, Halina E. Tegetmeyer, Dietmar Riedel, Hans-Hermann Richnow, Lorenz Adrian, Thorsten Reemtsma, Oliver J. Lechtenfeld and Florin Musat ()
Additional contact information
Rafael Laso-Pérez: Max-Planck Institute for Marine Microbiology
Gunter Wegener: Max-Planck Institute for Marine Microbiology
Katrin Knittel: Max-Planck Institute for Marine Microbiology
Friedrich Widdel: Max-Planck Institute for Marine Microbiology
Katie J. Harding: Max-Planck Institute for Marine Microbiology
Viola Krukenberg: Max-Planck Institute for Marine Microbiology
Dimitri V. Meier: Max-Planck Institute for Marine Microbiology
Michael Richter: Max-Planck Institute for Marine Microbiology
Halina E. Tegetmeyer: Alfred Wegener Institute Helmholtz Center for Polar and Marine Research
Dietmar Riedel: Max Planck Institute for Biophysical Chemistry
Hans-Hermann Richnow: Helmholtz Centre for Environmental Research − UFZ
Lorenz Adrian: Helmholtz Centre for Environmental Research − UFZ
Thorsten Reemtsma: Helmholtz Centre for Environmental Research − UFZ
Oliver J. Lechtenfeld: Helmholtz Centre for Environmental Research − UFZ
Florin Musat: Max-Planck Institute for Marine Microbiology

Nature, 2016, vol. 539, issue 7629, 396-401

Abstract: 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.

Date: 2016
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DOI: 10.1038/nature20152

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