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Thermophilic archaea activate butane via alkyl-coenzyme M formation
by
Musat, Florin
, Tegetmeyer, Halina E.
, Meier, Dimitri V.
, Lechtenfeld, Oliver J.
, Laso-Pérez, Rafael
, Widdel, Friedrich
, Richter, Michael
, Harding, Katie J.
, Krukenberg, Viola
, Knittel, Katrin
, Riedel, Dietmar
, Wegener, Gunter
, Richnow, Hans-Hermann
, Adrian, Lorenz
, Reemtsma, Thorsten
in
631/326/171
/ 631/326/26/2527
/ 631/45/320
/ Alkylation
/ Anaerobiosis
/ Archaea - genetics
/ Archaea - metabolism
/ Archaeabacteria
/ Archaeal Proteins - chemistry
/ Archaeal Proteins - genetics
/ Archaeal Proteins - metabolism
/ Bacteria
/ Biocatalysis
/ Butanes - metabolism
/ Carbon monoxide
/ Dehydrogenases
/ Enzymes
/ Evolution, Molecular
/ Gases
/ Genes
/ Genomes
/ Humanities and Social Sciences
/ Hydrocarbons
/ Mesna - chemistry
/ Mesna - metabolism
/ Metabolism
/ Methane
/ Methanogenesis
/ Microorganisms
/ multidisciplinary
/ Natural gas
/ Observations
/ Oxidation
/ Oxidation-Reduction
/ Physiological aspects
/ Science
/ Sediments
/ Sulfate reduction
/ Sulfates - metabolism
/ Temperature
2016
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Thermophilic archaea activate butane via alkyl-coenzyme M formation
by
Musat, Florin
, Tegetmeyer, Halina E.
, Meier, Dimitri V.
, Lechtenfeld, Oliver J.
, Laso-Pérez, Rafael
, Widdel, Friedrich
, Richter, Michael
, Harding, Katie J.
, Krukenberg, Viola
, Knittel, Katrin
, Riedel, Dietmar
, Wegener, Gunter
, Richnow, Hans-Hermann
, Adrian, Lorenz
, Reemtsma, Thorsten
in
631/326/171
/ 631/326/26/2527
/ 631/45/320
/ Alkylation
/ Anaerobiosis
/ Archaea - genetics
/ Archaea - metabolism
/ Archaeabacteria
/ Archaeal Proteins - chemistry
/ Archaeal Proteins - genetics
/ Archaeal Proteins - metabolism
/ Bacteria
/ Biocatalysis
/ Butanes - metabolism
/ Carbon monoxide
/ Dehydrogenases
/ Enzymes
/ Evolution, Molecular
/ Gases
/ Genes
/ Genomes
/ Humanities and Social Sciences
/ Hydrocarbons
/ Mesna - chemistry
/ Mesna - metabolism
/ Metabolism
/ Methane
/ Methanogenesis
/ Microorganisms
/ multidisciplinary
/ Natural gas
/ Observations
/ Oxidation
/ Oxidation-Reduction
/ Physiological aspects
/ Science
/ Sediments
/ Sulfate reduction
/ Sulfates - metabolism
/ Temperature
2016
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Thermophilic archaea activate butane via alkyl-coenzyme M formation
by
Musat, Florin
, Tegetmeyer, Halina E.
, Meier, Dimitri V.
, Lechtenfeld, Oliver J.
, Laso-Pérez, Rafael
, Widdel, Friedrich
, Richter, Michael
, Harding, Katie J.
, Krukenberg, Viola
, Knittel, Katrin
, Riedel, Dietmar
, Wegener, Gunter
, Richnow, Hans-Hermann
, Adrian, Lorenz
, Reemtsma, Thorsten
in
631/326/171
/ 631/326/26/2527
/ 631/45/320
/ Alkylation
/ Anaerobiosis
/ Archaea - genetics
/ Archaea - metabolism
/ Archaeabacteria
/ Archaeal Proteins - chemistry
/ Archaeal Proteins - genetics
/ Archaeal Proteins - metabolism
/ Bacteria
/ Biocatalysis
/ Butanes - metabolism
/ Carbon monoxide
/ Dehydrogenases
/ Enzymes
/ Evolution, Molecular
/ Gases
/ Genes
/ Genomes
/ Humanities and Social Sciences
/ Hydrocarbons
/ Mesna - chemistry
/ Mesna - metabolism
/ Metabolism
/ Methane
/ Methanogenesis
/ Microorganisms
/ multidisciplinary
/ Natural gas
/ Observations
/ Oxidation
/ Oxidation-Reduction
/ Physiological aspects
/ Science
/ Sediments
/ Sulfate reduction
/ Sulfates - metabolism
/ Temperature
2016
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Thermophilic archaea activate butane via alkyl-coenzyme M formation
Journal Article
Thermophilic archaea activate butane via alkyl-coenzyme M formation
2016
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Overview
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 β-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.
Anaerobic archaea enriched in thermophilic microbial consortia completely degrade butane by modifying mechanisms which were hitherto thought to be specific to methane metabolism.
Environmental oxidation of non-methane hydrocarbons
Research on the anaerobic oxidation of natural gas has largely been focused on methane as the most abundant constituent. It is less clear how short-chain alkanes—including ethane, propane,
n
-butane and
iso
-butane, which together make up about 20% of natural gas—are anaerobically metabolized. Sulfate-reducing bacteria are the only organisms known to date to anaerobically oxidize short-chain hydrocarbons. Gunter Wegener and colleagues identify an anaerobic thermophilic enrichment culture composed of dense consortia of archaea and bacteria that uses a pathway similar to anaerobic methane oxidation, which was previously thought to be specific for C
1
-compounds, to oxidize butane. Archaea activate butane, and reducing equivalents are channelled to sulfate-reducing partner bacteria. Similar consortia are detected in marine subsurface sediments, suggesting that this pathway may be widespread in nature.
Publisher
Nature Publishing Group UK,Nature Publishing Group
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