Anaerobic oxidation of saturated hydrocarbons to CO2 by a new type of sulfate-reducing bacterium

Aeckersberg, Frank; Bak, Friedhelm; Widdel, Friedrich

doi:10.1007/bf00418180

Cited by 401 publications

(221 citation statements)

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“…1). This analysis also shows that strain LM2801 T is distantly related to other alkene-oxidizing sulfate-reducing strains, including Hxd3 (Aeckersberg et al, 1991), Pnd3 (Aeckersberg et al, 1998), AK-01 (So & Young, 1999), Desulfatibacillum aliphaticivorans CV2803 T (Cravo-Laureau et al, 2004a) and Desulfatibacillum alkenivorans PF2803 T (Cravo-Laureau et al, 2004b) (Fig. 1), with less than 92 % 16S rRNA gene sequence identity.…”

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confidence: 81%

Desulfatiferula olefinivorans gen. nov., sp. nov., a long-chain n-alkene-degrading, sulfate-reducing bacterium

Cravo‐Laureau

Labat

Joulian

et al. 2007

International Journal of Systematic and Evolutionary Microbiology

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A novel anaerobic, long-chain alkene-degrading, sulfate-reducing bacterium, strain LM2801T, was isolated from brackish sediment of a wastewater decantation facility of an oil refinery (Berre lagoon, France). Cells of strain LM2801T were Gram-negative, motile, slightly curved or vibrioid rods. Its optimum growth conditions were 30–36 °C, 6–10 g NaCl l−1 and pH 7.5. Strain LM2801T incompletely oxidized long-chain alkenes (from C14 to C23) and fatty acids (C14 to C24). The DNA G+C content was 45.5 mol%. Sequence analyses of the 16S rRNA and dsrAB genes indicated that the strain was a member of the family Desulfobacteraceae within the Deltaproteobacteria. This novel isolate possesses phenotypic and phylogenetic traits that do not allow its classification as a member of any previously described genus. Therefore, strain LM2801T is described as a member of a new genus, Desulfatiferula gen. nov., of which Desulfatiferula olefinivorans sp. nov. is the type species. The type strain of Desulfatiferula olefinivorans is LM2801T (=DSM 18843T =JCM 14469T).

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mentioning

confidence: 81%

Desulfatiferula olefinivorans gen. nov., sp. nov., a long-chain n-alkene-degrading, sulfate-reducing bacterium

Cravo‐Laureau

Labat

Joulian

et al. 2007

International Journal of Systematic and Evolutionary Microbiology

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“…A 1-liter preculture was inoculated in a 10-liter vessel of carbonate-buffered mineral salt medium at pH 7.0. Filter-sterilized limonene and vitamins (25) were added after cooling, and the culture was incubated for 6 -7 days with a CO 2 /N 2 (10/90 (v/v)) gas stream of 24 ml h Ϫ1 at 28°C. The stirrer frequency was initially 150 rpm and was increased during exponential growth phase of C. defragrans up to 250 rpm to ensure optimal substrate availability.…”

Section: Methodsmentioning

confidence: 99%

Linalool Dehydratase-Isomerase, a Bifunctional Enzyme in the Anaerobic Degradation of Monoterpenes

Brodkorb

Gottschall

Marmulla

et al. 2010

Journal of Biological Chemistry

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Castellaniella (ex Alcaligenes) defragrans strain 65Phen mineralizes monoterpenes in the absence of oxygen. Soluble cell extracts anaerobically catalyzed the isomerization of geraniol to linalool and the dehydration of linalool to myrcene. The linalool dehydratase was present in cells grown on monoterpenes, but not if grown on acetate. We purified the novel enzyme ϳ1800-fold to complete homogeneity. The native enzyme had a molecular mass of 160 kDa. Denaturing gel electrophoresis revealed one single protein band with a molecular mass of 40 kDa, which indicated a homotetramer as native conformation. The aerobically purified enzyme was anaerobically activated in the presence of 2 mM DTT. The linalool dehydratase catalyzed in vitro two reactions in both directions depending on the thermodynamic driving forces: a water secession from the tertiary alcohol linalool to the corresponding acyclic monoterpene myrcene and an isomerization of the primary allylalcohol geraniol in its stereoisomer linalool. The specific activities (V max ) were 140 nanokatals mg ؊1 for the linalool dehydratase and 410 nanokatals mg ؊1 for the geraniol isomerase, with apparent K m values of 750 M and 500 M, respectively. The corresponding open reading frame was identified and revealed a precursor protein with a signal peptide for a periplasmatic location. The amino acid sequence did not affiliate with any described enzymes. We suggest naming the enzyme linalool dehydratase-isomerase according to its bifunctionality and placing it as a member of a new protein family within the hydrolyases (EC 4.2

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“…Methane was quantified in the headspace by gas chromatography (see above). Sulfide was liberated from ZnS (by acidification) and quantified colorimetrically using the methylene blue-forming reaction in a miniaturized assay (Aeckersberg et al, 1991).…”

Section: Enrichment Of Anaerobic Methanotrophic Microorganismsmentioning

confidence: 99%

Thermophilic anaerobic oxidation of methane by marine microbial consortia

Holler

Widdel

Knittel

et al. 2011

ISME J

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The anaerobic oxidation of methane (AOM) with sulfate controls the emission of the greenhouse gas methane from the ocean floor. AOM is performed by microbial consortia of archaea (ANME) associated with partners related to sulfate-reducing bacteria. In vitro enrichments of AOM were so far only successful at temperatures p25 1C; however, energy gain for growth by AOM with sulfate is in principle also possible at higher temperatures. Sequences of 16S rRNA genes and core lipids characteristic for ANME as well as hints of in situ AOM activity were indeed reported for geothermally heated marine environments, yet no direct evidence for thermophilic growth of marine ANME consortia was obtained to date. To study possible thermophilic AOM, we investigated hydrothermally influenced sediment from the Guaymas Basin. In vitro incubations showed activity of sulfate-dependent methane oxidation between 5 and 70 1C with an apparent optimum between 45 and 60 1C. AOM was absent at temperatures X75 1C. Long-term enrichment of AOM was fastest at 50 1C, yielding a 13-fold increase of methane-dependent sulfate reduction within 250 days, equivalent to an apparent doubling time of 68 days. The enrichments were dominated by novel ANME-1 consortia, mostly associated with bacterial partners of the deltaproteobacterial HotSeep-1 cluster, a deeply branching phylogenetic group previously found in a butane-amended 60 1C-enrichment culture of Guaymas sediments. The closest relatives (Desulfurella spp.; Hippea maritima) are moderately thermophilic sulfur reducers. Results indicate that AOM and ANME archaea could be of biogeochemical relevance not only in cold to moderate but also in hot marine habitats.

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Anaerobic oxidation of saturated hydrocarbons to CO2 by a new type of sulfate-reducing bacterium

Cited by 401 publications

References 38 publications

Desulfatiferula olefinivorans gen. nov., sp. nov., a long-chain n-alkene-degrading, sulfate-reducing bacterium

Desulfatiferula olefinivorans gen. nov., sp. nov., a long-chain n-alkene-degrading, sulfate-reducing bacterium

Linalool Dehydratase-Isomerase, a Bifunctional Enzyme in the Anaerobic Degradation of Monoterpenes

Thermophilic anaerobic oxidation of methane by marine microbial consortia

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