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Gabriele Diekert - One of the best experts on this subject based on the ideXlab platform.
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Selective, light-driven enzymatic dehalogenations of organic compounds
RSC Advances, 2020Co-Authors: Bhavin Siritanaratkul, Tobias Goris, Gabriele Diekert, Torsten Schubert, Shams T. A. Islam, Cindy Kunze, Fraser A. ArmstrongAbstract:Tetrachloroethene reductive dehalogenase (PceA), a corrinoid-containing enzyme from Sulfurospirillum multivorans, is highly active for the sequential reduction of the organohalide tetrachloroethene (PCE) to trichloroethene (TCE), then regiospecifically to cis-1,2-dichloroethene (cDCE). We demonstrate direct electron transfer from graphite and semiconductor electrodes to PceA adsorbed onto the electrode surface. Colloidal TiO2 nanoparticles modified with PceA efficiently carry out the sequence of dehalogenation reactions under UV light irradiation.
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Hydrogen production by Sulfurospirillum species enables syntrophic interactions of Epsilonproteobacteria.
Nature Communications, 2018Co-Authors: Stefan Kruse, Tobias Goris, Martin Westermann, Lorenz Adrian, Gabriele DiekertAbstract:Hydrogen-producing bacteria are of environmental importance, since hydrogen is a major electron donor for prokaryotes in anoxic ecosystems. Epsilonproteobacteria are currently considered to be hydrogen-oxidizing bacteria exclusively. Here, we report hydrogen production upon pyruvate fermentation for free-living Epsilonproteobacteria, Sulfurospirillum spp. The amount of hydrogen produced is different in two subgroups of Sulfurospirillum spp., represented by S. cavolei and S. multivorans. The former produces more hydrogen and excretes acetate as sole organic acid, while the latter additionally produces lactate and succinate. Hydrogen production can be assigned by differential proteomics to a hydrogenase (similar to hydrogenase 4 from E. coli) that is more abundant during fermentation. A syntrophic interaction is established between Sulfurospirillum multivorans and Methanococcus voltae when cocultured with lactate as sole substrate, as the former cannot grow fermentatively on lactate alone and the latter relies on hydrogen for growth. This might hint to a yet unrecognized role of Epsilonproteobacteria as hydrogen producers in anoxic microbial communities. Epsilonproteobacteria, such as Sulfurospirillum, can use molecular hydrogen as an electron donor for respiration. Here, the authors show that Sulfurospirillum can, in addition, release hydrogen during fermentation, allowing metabolic interactions with other hydrogen-consuming microorganisms.
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hydrogen production by Sulfurospirillum species enables syntrophic interactions of epsilonproteobacteria
Nature Communications, 2018Co-Authors: Stefan Kruse, Tobias Goris, Martin Westermann, Lorenz Adrian, Gabriele DiekertAbstract:Hydrogen-producing bacteria are of environmental importance, since hydrogen is a major electron donor for prokaryotes in anoxic ecosystems. Epsilonproteobacteria are currently considered to be hydrogen-oxidizing bacteria exclusively. Here, we report hydrogen production upon pyruvate fermentation for free-living Epsilonproteobacteria, Sulfurospirillum spp. The amount of hydrogen produced is different in two subgroups of Sulfurospirillum spp., represented by S. cavolei and S. multivorans. The former produces more hydrogen and excretes acetate as sole organic acid, while the latter additionally produces lactate and succinate. Hydrogen production can be assigned by differential proteomics to a hydrogenase (similar to hydrogenase 4 from E. coli) that is more abundant during fermentation. A syntrophic interaction is established between Sulfurospirillum multivorans and Methanococcus voltae when cocultured with lactate as sole substrate, as the former cannot grow fermentatively on lactate alone and the latter relies on hydrogen for growth. This might hint to a yet unrecognized role of Epsilonproteobacteria as hydrogen producers in anoxic microbial communities.
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Biosynthesis, Synthesis, and Activities of Barnesin A, a NRPS-PKS Hybrid Produced by an Anaerobic Epsilonproteobacterium.
ACS Chemical Biology, 2018Co-Authors: Maja Rischer, Tobias Goris, Gabriele Diekert, Luka Raguž, Francois Keiff, Christine BeemelmannsAbstract:Despite the wealth of physiological knowledge and plentiful genomes available, only few natural products of anaerobic bacteria have been identified until today and even less have been linked to their biosynthetic gene cluster. Here, we analyzed a unique NRPS-PKS hybrid gene cluster from an anaerobic Epsilonproteobacterium (Sulfurospirillum barnesii). Phylogenetic analysis of key biosynthetic genes, gene expression studies, and comparative metabolomics resulted in the identification of the first anoxically biosynthesized NRPS-PKS hybrid metabolite: a lipo-dipeptide with a vinylogous side chain, called barnesin A. The absolute structure was verified by a modular total synthesis, and barnesin and derivatives were found to have antimicrobial activity, as well as selective and nanomolar inhibitory activity, against pharmacological important cysteine proteases, such as cathepsin B.
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a retentive memory of tetrachloroethene respiration in Sulfurospirillum halorespirans involved proteins and a possible link to acetylation of a two component regulatory system
Journal of Proteomics, 2018Co-Authors: Dominique Turkowsky, Tobias Goris, Gabriele Diekert, Torsten Schubert, Jens Esken, Nico Jehmlich, Martin Von BergenAbstract:Abstract Organohalide respiration (OHR), comprising the reductive dehalogenation of halogenated organic compounds, is subject to a unique memory effect and long-term transcriptional downregulation of the involved genes in Sulfurospirillum multivorans . Gene expression ceases slowly over approximately 100 generations in the absence of tetrachloroethene (PCE). However, the molecular mechanisms of this regulation process are not understood. We show here that Sulfurospirillum halorespirans undergoes the same type of regulation when cultivated without chlorinated ethenes for a long period of time. In addition, we compared the proteomes of S. halorespirans cells cultivated in the presence of PCE with those of cells long- and short-term cultivated with nitrate as the sole electron acceptor. Important OHR-related proteins previously unidentified in S. multivorans include a histidine kinase, a putative quinol dehydrogenase membrane protein, and a PCE-induced porin. Since for some regulatory proteins a posttranslational regulation of activity by lysine acetylations is known, we also analyzed the acetylome of S. halorespirans , revealing that 32% of the proteome was acetylated in at least one condition. The data indicate that the response regulator and the histidine kinase of a two-component system most probably involved in induction of PCE respiration are highly acetylated during short-term cultivation with nitrate in the absence of PCE. Significance The so far unique long-term downregulation of organohalide respiration is now identified in a second species suggesting a broader distribution of this regulatory phenomenon. An improved protein extraction method allowed the identification of proteins most probably involved in transcriptional regulation of OHR in Sulfurospirillum spp. Our data indicate that acetylations of regulatory proteins are involved in this extreme, sustained standby-mode of metabolic enzymes in the absence of a substrate. This first published acetylome of Epsilonproteobacteria might help to study other ecologically or medically important species of this clade.
Torsten Schubert - One of the best experts on this subject based on the ideXlab platform.
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Selective, light-driven enzymatic dehalogenations of organic compounds
RSC Advances, 2020Co-Authors: Bhavin Siritanaratkul, Tobias Goris, Gabriele Diekert, Torsten Schubert, Shams T. A. Islam, Cindy Kunze, Fraser A. ArmstrongAbstract:Tetrachloroethene reductive dehalogenase (PceA), a corrinoid-containing enzyme from Sulfurospirillum multivorans, is highly active for the sequential reduction of the organohalide tetrachloroethene (PCE) to trichloroethene (TCE), then regiospecifically to cis-1,2-dichloroethene (cDCE). We demonstrate direct electron transfer from graphite and semiconductor electrodes to PceA adsorbed onto the electrode surface. Colloidal TiO2 nanoparticles modified with PceA efficiently carry out the sequence of dehalogenation reactions under UV light irradiation.
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Functional diversity of reductive dehalogenases in a bacterial consortium degrading chloroethenes
2020Co-Authors: Géraldine Florence Buttet, Christof Holliger, Torsten Schubert, Cindy Kunze, Sebastian Keller, Julien MaillardAbstract:Chlorinated hydrocarbon pollution threatens nature and human health due to its toxic and carcinogenic potential. Enrichment cultures were investigated for the bioremediation potential of tetrachloroethene (PCE). This process is based on bacterial anaerobic respiration in which the chlorinated compounds are used as electron acceptors (organohalide respiration, OHR). The key enzyme in OHR is the reductive dehalogenase (rdhA), which contains a corrinoid as cofactor. This study is focused on a better understanding of the functional diversity of rdhA genes and the interplay of OHR bacterial populations during PCE dechlorination. Two bacterial consortia containing different members of the Sulfurospirillum genus are investigated in our laboratory. The specificity in these consortia resides in the fact that although both producing highly similar RdhA enzymes, they catalyze reduction of PCE with different rate and substrate specificity. The culture harboring the enzyme PceATCE showed a higher PCE dechlorination activity and is involved in the dechlorination of PCE to trichloroethene (TCE), exclusively, whereas the culture which contains the enzyme PceADCE is able to dechlorinate PCE via TCE to cis-dichloroethene (cDCE). Corrinoid extraction data suggested that the corrinoid cofactor present in PceATCE is norpseudo-B12 as in the well-characterized PceA of S. multivorans which dechlorinates PCE to cDCE. Sulfurospirillum spp. are versatile OHR bacteria, therefore the question of rdhA gene regulation needs to be investigated. Pulse experiments with chloroethenes are performed on those consortia growing on fumarate as an alternative electron acceptor, followed by RNA extraction and qPCR analysis targeting genes involved in OHR metabolism. In addition, the competition of both dechlorinating populations for the substrate PCE is assessed by mixing them with different ratios and following their growth and activity. This should further help understanding the molecular basis of substrate affinity and specificity of the two RdhA enzymes present.
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Structural and functional analysis of an l-serine O-phosphate decarboxylase involved in norcobamide biosynthesis.
FEBS Letters, 2019Co-Authors: Sebastian Keller, Karl M. Wetterhorn, Alison Vecellio, Mark Seeger, Ivan Rayment, Torsten SchubertAbstract:Structural diversity of natural cobamides (Cbas, B12 vitamers) is limited to the nucleotide loop. The loop is connected to the cobalt-containing corrin ring via an (R)-1-aminopropan-2-ol O-2-phosphate (AP-P) linker moiety. AP-P is produced by the l-threonine O-3-phosphate (l-Thr-P) decarboxylase CobD. Here, the CobD homolog SMUL_1544 of the organohalide-respiring epsilonproteobacterium Sulfurospirillum multivorans was characterized as a decarboxylase that produces ethanolamine O-phosphate (EA-P) from l-serine O-phosphate (l-Ser-P). EA-P is assumed to serve as precursor of the linker moiety of norcobamides that function as cofactors in the respiratory reductive dehalogenase. SMUL_1544 (SmCobD) is a pyridoxal-5'-phosphate (PLP)-containing enzyme. The structural analysis of the SmCobD apoprotein combined with the characterization of truncated mutant proteins uncovered a role of the SmCobD N-terminus in efficient l-Ser-P conversion.
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a retentive memory of tetrachloroethene respiration in Sulfurospirillum halorespirans involved proteins and a possible link to acetylation of a two component regulatory system
Journal of Proteomics, 2018Co-Authors: Dominique Turkowsky, Tobias Goris, Gabriele Diekert, Torsten Schubert, Jens Esken, Nico Jehmlich, Martin Von BergenAbstract:Abstract Organohalide respiration (OHR), comprising the reductive dehalogenation of halogenated organic compounds, is subject to a unique memory effect and long-term transcriptional downregulation of the involved genes in Sulfurospirillum multivorans . Gene expression ceases slowly over approximately 100 generations in the absence of tetrachloroethene (PCE). However, the molecular mechanisms of this regulation process are not understood. We show here that Sulfurospirillum halorespirans undergoes the same type of regulation when cultivated without chlorinated ethenes for a long period of time. In addition, we compared the proteomes of S. halorespirans cells cultivated in the presence of PCE with those of cells long- and short-term cultivated with nitrate as the sole electron acceptor. Important OHR-related proteins previously unidentified in S. multivorans include a histidine kinase, a putative quinol dehydrogenase membrane protein, and a PCE-induced porin. Since for some regulatory proteins a posttranslational regulation of activity by lysine acetylations is known, we also analyzed the acetylome of S. halorespirans , revealing that 32% of the proteome was acetylated in at least one condition. The data indicate that the response regulator and the histidine kinase of a two-component system most probably involved in induction of PCE respiration are highly acetylated during short-term cultivation with nitrate in the absence of PCE. Significance The so far unique long-term downregulation of organohalide respiration is now identified in a second species suggesting a broader distribution of this regulatory phenomenon. An improved protein extraction method allowed the identification of proteins most probably involved in transcriptional regulation of OHR in Sulfurospirillum spp. Our data indicate that acetylations of regulatory proteins are involved in this extreme, sustained standby-mode of metabolic enzymes in the absence of a substrate. This first published acetylome of Epsilonproteobacteria might help to study other ecologically or medically important species of this clade.
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selective utilization of benzimidazolyl norcobamides as cofactors by the tetrachloroethene reductive dehalogenase of Sulfurospirillum multivorans
Journal of Bacteriology, 2018Co-Authors: Sebastian Keller, Cindy Kunze, Martin Bommer, Holger Dobbek, Ales Svatos, Christian Paetz, Riya Christina Menezes, Torsten SchubertAbstract:ABSTRACT The organohalide-respiring bacterium Sulfurospirillum multivorans produces a unique cobamide, namely, norpseudo-B12, which serves as cofactor of the tetrachloroethene (PCE) reductive dehalogenase (PceA). As previously reported, a replacement of the adeninyl moiety, the lower base of the cofactor, by exogenously applied 5,6-dimethylbenzimidazole led to inactive PceA. To explore the general effect of benzimidazoles on the PCE metabolism, the susceptibility of the organism for guided biosynthesis of various singly substituted benzimidazolyl-norcobamides was investigated, and their use as cofactor by PceA was analyzed. Exogenously applied 5-methylbenzimidazole (5-MeBza), 5-hydroxybenzimidazole (5-OHBza), and 5-methoxybenzimidazole (5-OMeBza) were found to be efficiently incorporated as lower bases into norcobamides (NCbas). Structural analysis of the NCbas by nuclear magnetic resonance spectroscopy uncovered a regioselectivity in the utilization of these precursors for NCba biosynthesis. When 5-MeBza was added, a mixture of 5-MeBza-norcobamide and 6-MeBza-norcobamide was formed, and the PceA enzyme activity was affected. In the presence of 5-OHBza, almost exclusively 6-OHBza-norcobamide was produced, while in the presence of 5-OMeBza, predominantly 5-OMeBza-norcobamide was detected. Both NCbas were incorporated into PceA, and no negative effect on the PceA activity was observed. In crystal structures of PceA, both NCbas were bound in the base-off mode with the 6-OHBza and 5-OMeBza lower bases accommodated by the same solvent-exposed hydrophilic pocket that harbors the adenine as the lower base of authentic norpseudo-B12. In this study, a selective production of different norcobamide isomers containing singly substituted benzimidazoles as lower bases is shown, and unique structural insights into their utilization as cofactors by a cobamide-containing enzyme are provided. IMPORTANCE Guided biosynthesis of norcobamides containing singly substituted benzimidazoles as lower bases by the organohalide-respiring epsilonproteobacterium Sulfurospirillum multivorans is reported. An unprecedented specificity in the formation of norcobamide isomers containing hydroxylated or methoxylated benzimidazoles was observed that implicated a strict regioselectivity of the norcobamide biosynthesis in the organism. In contrast to 5,6-dimethylbenzimidazolyl-norcobamide, the incorporation of singly substituted benzimidazolyl-norcobamides as a cofactor into the tetrachloroethene reductive dehalogenase was not impaired. The enzyme was found to be functional with different isomers and not limited to the use of adeninyl-norcobamide. Structural analysis of the enzyme equipped with either adeninyl- or benzimidazolyl-norcobamide cofactors visualized for the first time structurally different cobamides bound in base-off conformation to the cofactor-binding site of a cobamide-containing enzyme.
Tobias Goris - One of the best experts on this subject based on the ideXlab platform.
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Selective, light-driven enzymatic dehalogenations of organic compounds
RSC Advances, 2020Co-Authors: Bhavin Siritanaratkul, Tobias Goris, Gabriele Diekert, Torsten Schubert, Shams T. A. Islam, Cindy Kunze, Fraser A. ArmstrongAbstract:Tetrachloroethene reductive dehalogenase (PceA), a corrinoid-containing enzyme from Sulfurospirillum multivorans, is highly active for the sequential reduction of the organohalide tetrachloroethene (PCE) to trichloroethene (TCE), then regiospecifically to cis-1,2-dichloroethene (cDCE). We demonstrate direct electron transfer from graphite and semiconductor electrodes to PceA adsorbed onto the electrode surface. Colloidal TiO2 nanoparticles modified with PceA efficiently carry out the sequence of dehalogenation reactions under UV light irradiation.
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Hydrogen production by Sulfurospirillum species enables syntrophic interactions of Epsilonproteobacteria.
Nature Communications, 2018Co-Authors: Stefan Kruse, Tobias Goris, Martin Westermann, Lorenz Adrian, Gabriele DiekertAbstract:Hydrogen-producing bacteria are of environmental importance, since hydrogen is a major electron donor for prokaryotes in anoxic ecosystems. Epsilonproteobacteria are currently considered to be hydrogen-oxidizing bacteria exclusively. Here, we report hydrogen production upon pyruvate fermentation for free-living Epsilonproteobacteria, Sulfurospirillum spp. The amount of hydrogen produced is different in two subgroups of Sulfurospirillum spp., represented by S. cavolei and S. multivorans. The former produces more hydrogen and excretes acetate as sole organic acid, while the latter additionally produces lactate and succinate. Hydrogen production can be assigned by differential proteomics to a hydrogenase (similar to hydrogenase 4 from E. coli) that is more abundant during fermentation. A syntrophic interaction is established between Sulfurospirillum multivorans and Methanococcus voltae when cocultured with lactate as sole substrate, as the former cannot grow fermentatively on lactate alone and the latter relies on hydrogen for growth. This might hint to a yet unrecognized role of Epsilonproteobacteria as hydrogen producers in anoxic microbial communities. Epsilonproteobacteria, such as Sulfurospirillum, can use molecular hydrogen as an electron donor for respiration. Here, the authors show that Sulfurospirillum can, in addition, release hydrogen during fermentation, allowing metabolic interactions with other hydrogen-consuming microorganisms.
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hydrogen production by Sulfurospirillum species enables syntrophic interactions of epsilonproteobacteria
Nature Communications, 2018Co-Authors: Stefan Kruse, Tobias Goris, Martin Westermann, Lorenz Adrian, Gabriele DiekertAbstract:Hydrogen-producing bacteria are of environmental importance, since hydrogen is a major electron donor for prokaryotes in anoxic ecosystems. Epsilonproteobacteria are currently considered to be hydrogen-oxidizing bacteria exclusively. Here, we report hydrogen production upon pyruvate fermentation for free-living Epsilonproteobacteria, Sulfurospirillum spp. The amount of hydrogen produced is different in two subgroups of Sulfurospirillum spp., represented by S. cavolei and S. multivorans. The former produces more hydrogen and excretes acetate as sole organic acid, while the latter additionally produces lactate and succinate. Hydrogen production can be assigned by differential proteomics to a hydrogenase (similar to hydrogenase 4 from E. coli) that is more abundant during fermentation. A syntrophic interaction is established between Sulfurospirillum multivorans and Methanococcus voltae when cocultured with lactate as sole substrate, as the former cannot grow fermentatively on lactate alone and the latter relies on hydrogen for growth. This might hint to a yet unrecognized role of Epsilonproteobacteria as hydrogen producers in anoxic microbial communities.
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Biosynthesis, Synthesis, and Activities of Barnesin A, a NRPS-PKS Hybrid Produced by an Anaerobic Epsilonproteobacterium.
ACS Chemical Biology, 2018Co-Authors: Maja Rischer, Tobias Goris, Gabriele Diekert, Luka Raguž, Francois Keiff, Christine BeemelmannsAbstract:Despite the wealth of physiological knowledge and plentiful genomes available, only few natural products of anaerobic bacteria have been identified until today and even less have been linked to their biosynthetic gene cluster. Here, we analyzed a unique NRPS-PKS hybrid gene cluster from an anaerobic Epsilonproteobacterium (Sulfurospirillum barnesii). Phylogenetic analysis of key biosynthetic genes, gene expression studies, and comparative metabolomics resulted in the identification of the first anoxically biosynthesized NRPS-PKS hybrid metabolite: a lipo-dipeptide with a vinylogous side chain, called barnesin A. The absolute structure was verified by a modular total synthesis, and barnesin and derivatives were found to have antimicrobial activity, as well as selective and nanomolar inhibitory activity, against pharmacological important cysteine proteases, such as cathepsin B.
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a retentive memory of tetrachloroethene respiration in Sulfurospirillum halorespirans involved proteins and a possible link to acetylation of a two component regulatory system
Journal of Proteomics, 2018Co-Authors: Dominique Turkowsky, Tobias Goris, Gabriele Diekert, Torsten Schubert, Jens Esken, Nico Jehmlich, Martin Von BergenAbstract:Abstract Organohalide respiration (OHR), comprising the reductive dehalogenation of halogenated organic compounds, is subject to a unique memory effect and long-term transcriptional downregulation of the involved genes in Sulfurospirillum multivorans . Gene expression ceases slowly over approximately 100 generations in the absence of tetrachloroethene (PCE). However, the molecular mechanisms of this regulation process are not understood. We show here that Sulfurospirillum halorespirans undergoes the same type of regulation when cultivated without chlorinated ethenes for a long period of time. In addition, we compared the proteomes of S. halorespirans cells cultivated in the presence of PCE with those of cells long- and short-term cultivated with nitrate as the sole electron acceptor. Important OHR-related proteins previously unidentified in S. multivorans include a histidine kinase, a putative quinol dehydrogenase membrane protein, and a PCE-induced porin. Since for some regulatory proteins a posttranslational regulation of activity by lysine acetylations is known, we also analyzed the acetylome of S. halorespirans , revealing that 32% of the proteome was acetylated in at least one condition. The data indicate that the response regulator and the histidine kinase of a two-component system most probably involved in induction of PCE respiration are highly acetylated during short-term cultivation with nitrate in the absence of PCE. Significance The so far unique long-term downregulation of organohalide respiration is now identified in a second species suggesting a broader distribution of this regulatory phenomenon. An improved protein extraction method allowed the identification of proteins most probably involved in transcriptional regulation of OHR in Sulfurospirillum spp. Our data indicate that acetylations of regulatory proteins are involved in this extreme, sustained standby-mode of metabolic enzymes in the absence of a substrate. This first published acetylome of Epsilonproteobacteria might help to study other ecologically or medically important species of this clade.
Kazuya Watanabe - One of the best experts on this subject based on the ideXlab platform.
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Sulfurospirillum cavolei sp. nov., a facultatively anaerobic sulfur-reducing bacterium isolated from an underground crude oil storage cavity.
International journal of systematic and evolutionary microbiology, 2020Co-Authors: Yumiko Kodama, Le Thu Ha, Kazuya WatanabeAbstract:A novel facultatively anaerobic sulfur-reducing bacterium, designated strain Phe91(T), was isolated from petroleum-contaminated groundwater in an underground crude oil storage cavity at Kuji in Iwate, Japan. Cells of strain Phe91(T) were slightly curved rods with single polar flagella. Optimum growth was observed at pH 7.0 and 30 degrees C. The novel strain utilized elemental sulfur, thiosulfate, sulfite, dithionite, arsenate, nitrate and DMSO as electron acceptors with lactate as an energy and carbon source, but nitrite was not utilized. Microaerophilic growth was also observed. Fumarate, pyruvate, lactate, malate, succinate, hydrogen (with acetate as a carbon source) and formate (with acetate) could serve as electron donors. Fumarate, pyruvate and malate were fermented. The DNA G+C content was 42.7 mol%. On the basis of 16S rRNA gene sequence phylogeny, strain Phe91(T) was affiliated with the genus Sulfurospirillum in the class Epsilonproteobacteria and was most closely related to Sulfurospirillum deleyianum (sequence similarity 97 %). However, the DNA-DNA hybridization value between strain Phe91(T) and S. deleyianum was only 14 %. Based on the physiological and phylogenetic data, Phe91(T) should be classified as a representative of a novel species in the genus Sulfurospirillum; the name Sulfurospirillum cavolei sp. nov. is proposed, with Phe91(T) (=JCM 13918(T)=DSM 18149(T)) as the type strain.
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Sulfurospirillum cavolei sp nov a facultatively anaerobic sulfur reducing bacterium isolated from an underground crude oil storage cavity
International Journal of Systematic and Evolutionary Microbiology, 2007Co-Authors: Yumiko Kodama, Le Thu Ha, Kazuya WatanabeAbstract:A novel facultatively anaerobic sulfur-reducing bacterium, designated strain Phe91T, was isolated from petroleum-contaminated groundwater in an underground crude oil storage cavity at Kuji in Iwate, Japan. Cells of strain Phe91T were slightly curved rods with single polar flagella. Optimum growth was observed at pH 7.0 and 30 °C. The novel strain utilized elemental sulfur, thiosulfate, sulfite, dithionite, arsenate, nitrate and DMSO as electron acceptors with lactate as an energy and carbon source, but nitrite was not utilized. Microaerophilic growth was also observed. Fumarate, pyruvate, lactate, malate, succinate, hydrogen (with acetate as a carbon source) and formate (with acetate) could serve as electron donors. Fumarate, pyruvate and malate were fermented. The DNA G+C content was 42.7 mol%. On the basis of 16S rRNA gene sequence phylogeny, strain Phe91T was affiliated with the genus Sulfurospirillum in the class Epsilonproteobacteria and was most closely related to Sulfurospirillum deleyianum (sequence similarity 97 %). However, the DNA–DNA hybridization value between strain Phe91T and S. deleyianum was only 14 %. Based on the physiological and phylogenetic data, Phe91T should be classified as a representative of a novel species in the genus Sulfurospirillum; the name Sulfurospirillum cavolei sp. nov. is proposed, with Phe91T (=JCM 13918T=DSM 18149T) as the type strain.
Le Thu Ha - One of the best experts on this subject based on the ideXlab platform.
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Sulfurospirillum cavolei sp. nov., a facultatively anaerobic sulfur-reducing bacterium isolated from an underground crude oil storage cavity.
International journal of systematic and evolutionary microbiology, 2020Co-Authors: Yumiko Kodama, Le Thu Ha, Kazuya WatanabeAbstract:A novel facultatively anaerobic sulfur-reducing bacterium, designated strain Phe91(T), was isolated from petroleum-contaminated groundwater in an underground crude oil storage cavity at Kuji in Iwate, Japan. Cells of strain Phe91(T) were slightly curved rods with single polar flagella. Optimum growth was observed at pH 7.0 and 30 degrees C. The novel strain utilized elemental sulfur, thiosulfate, sulfite, dithionite, arsenate, nitrate and DMSO as electron acceptors with lactate as an energy and carbon source, but nitrite was not utilized. Microaerophilic growth was also observed. Fumarate, pyruvate, lactate, malate, succinate, hydrogen (with acetate as a carbon source) and formate (with acetate) could serve as electron donors. Fumarate, pyruvate and malate were fermented. The DNA G+C content was 42.7 mol%. On the basis of 16S rRNA gene sequence phylogeny, strain Phe91(T) was affiliated with the genus Sulfurospirillum in the class Epsilonproteobacteria and was most closely related to Sulfurospirillum deleyianum (sequence similarity 97 %). However, the DNA-DNA hybridization value between strain Phe91(T) and S. deleyianum was only 14 %. Based on the physiological and phylogenetic data, Phe91(T) should be classified as a representative of a novel species in the genus Sulfurospirillum; the name Sulfurospirillum cavolei sp. nov. is proposed, with Phe91(T) (=JCM 13918(T)=DSM 18149(T)) as the type strain.
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Sulfurospirillum cavolei sp nov a facultatively anaerobic sulfur reducing bacterium isolated from an underground crude oil storage cavity
International Journal of Systematic and Evolutionary Microbiology, 2007Co-Authors: Yumiko Kodama, Le Thu Ha, Kazuya WatanabeAbstract:A novel facultatively anaerobic sulfur-reducing bacterium, designated strain Phe91T, was isolated from petroleum-contaminated groundwater in an underground crude oil storage cavity at Kuji in Iwate, Japan. Cells of strain Phe91T were slightly curved rods with single polar flagella. Optimum growth was observed at pH 7.0 and 30 °C. The novel strain utilized elemental sulfur, thiosulfate, sulfite, dithionite, arsenate, nitrate and DMSO as electron acceptors with lactate as an energy and carbon source, but nitrite was not utilized. Microaerophilic growth was also observed. Fumarate, pyruvate, lactate, malate, succinate, hydrogen (with acetate as a carbon source) and formate (with acetate) could serve as electron donors. Fumarate, pyruvate and malate were fermented. The DNA G+C content was 42.7 mol%. On the basis of 16S rRNA gene sequence phylogeny, strain Phe91T was affiliated with the genus Sulfurospirillum in the class Epsilonproteobacteria and was most closely related to Sulfurospirillum deleyianum (sequence similarity 97 %). However, the DNA–DNA hybridization value between strain Phe91T and S. deleyianum was only 14 %. Based on the physiological and phylogenetic data, Phe91T should be classified as a representative of a novel species in the genus Sulfurospirillum; the name Sulfurospirillum cavolei sp. nov. is proposed, with Phe91T (=JCM 13918T=DSM 18149T) as the type strain.
