Thermophilic archaea activate butane via alkyl-coenzyme M formation
Laso-Pérez, R.; Wegener, G.; Knittel, K.; Widdel, F.; Harding, K.J.; Krukenberg, V.; Meier, D.V.; Richter, M.; Tegetmeyer, H.E.; Riedel, D.; Richnow, H.-H.; Adrian, L.; Reemtsma, T.; Lechtenfeld, O.J.; Musat, F. (2016). Thermophilic archaea activate butane via alkyl-coenzyme M formation. Nature (Lond.) 539(7629): 396-401. http://dx.doi.org/10.1038/nature20152
In: Nature: International Weekly Journal of Science. Nature Publishing Group: London. ISSN 0028-0836; e-ISSN 1476-4687, more
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| Authors | | Top |
- Laso-Pérez, R.
- Wegener, G.
- Knittel, K.
- Widdel, F., more
- Harding, K.J.
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- Krukenberg, V.
- Meier, D.V.
- Richter, M.
- Tegetmeyer, H.E.
- Riedel, D.
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- Richnow, H.-H.
- Adrian, L.
- Reemtsma, T.
- Lechtenfeld, O.J.
- Musat, F.
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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 C-1-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 C-4 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 beta-oxidation enzymes, carbon monoxide dehydrogenase and reversible C-1 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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