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  • 1
    Electronic Resource
    Electronic Resource
    Oxidation of organic compounds to CO2 with sulfur or thiosulfate as electron acceptor in the anaerobic hyperthermophilic archaea Thermoproteus tenax and Pyrobaculum islandicum proceeds via the citric acid cycle (1994)
    Springer
    Archives of microbiology 162 (1994), S. 286-294 
    Details
    ISSN: 1432-072X
    Keywords: Key words     Thermoproteus tenax ; Pyrobaculum ; islandicum ; Hyperthermophiles ; Archaea ; Acetyl-CoA oxidation ; Citric acid cycle ; Sulfur respiration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract      The oxidation of organic compounds with elemental sulfur or thiosulfate as electron acceptor was studied in the anaerobic hyperthermophilic archaea Thermoproteus tenax and Pyrobaculum islandicum. T. tenax was grown on either glucose or casamino acids and sulfur; P. islandicum on peptone and either elemental sulfur or thiosulfate as electron acceptor. During exponential growth only CO 2 and H2S rather than acetate, alanine, lactate, and succinate were detected as fermentation products of both organisms; the ratio of CO2/H2S formed was 1 : 2 with elemental sulfur and 1 : 1 with thiosulfate as electron acceptor. Cell extracts of T. tenax and P. islandicum contained all enzymes of the citric acid cycle in catabolic activities: citrate synthase, aconitase, isocitrate dehydrogenase (NADP+ -reducing), oxoglutarate : benzylviologen oxidoreductase, succinyl-CoA synthetase, succinate dehydrogenase, fumarase and malate dehydrogenase (NAD+-reducing). Carbon monoxide dehydrogenase activity was not detected. We conclude that in T. tenax and P. islandicum organic compounds are completely oxidized to CO2 with sulfur or thiosulfate as electron acceptor and that acetyl-CoA oxidation to CO2 proceeds via the citric acid cycle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00301853
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  • 2
    Electronic Resource
    Electronic Resource
    Oxidation of organic compounds to CO2 with sulfur or thiosulfate as electron acceptor in the anaerobic hyperthermophilic archaea Thermoproteus tenax and Pyrobaculum islandicum proceeds via the citric acid cycle (1994)
    Springer
    Archives of microbiology 162 (1994), S. 286-294 
    Details
    ISSN: 1432-072X
    Keywords: Thermoproteus tenax ; Pyrobaculum islandicum ; Hyperthermophiles ; Archaea ; Acetyl-CoA oxidation ; Citric acid cycle ; Sulfur respiration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The oxidation of organic compounds with elemental sulfur or thiosulfate as electron acceptor was studied in the anaerobic hyperthermophilic archaea Thermoproteus tenax and Pyrobaculum islandicum. T. tenax was grown on either glucose or casamino acids and sulfur; P. islandicum on peptone and either elemental sulfur or thiosulfate as electron acceptor. During exponential growth only CO2 and H2S rather than acetate, alanine, lactate, and succinate were detected as fermentation products of both organisms; the ratio of CO2/H2S formed was 1:2 with elemental sulfur and 1:1 with thiosulfate as electron acceptor. Cell extracts of T. tenax and P. islandicum contained all enzymes of the citric acid cycle in catabolic activities: citrate synthase, aconitase, isocitrate dehydrogenase (NADP+-reducing), oxoglutarate: benzylviologen oxidoreductase, succinyl-CoA synthetase, succinate dehydrogenase, fumarase and malate dehydrogenase (NAD+-reducing). Carbon monoxide dehydrogenase activity was not detected. We conclude that in T. tenax and P. islandicum organic compounds are completely oxidized to CO2 with sulfur or thiosulfate as electron acceptor and that acetyl-CoA oxidation to CO2 proceeds via the citric acid cycle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00301853
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  • 3
    Electronic Resource
    Electronic Resource
    Glucose fermentation to acetate, CO2 and H2 in the anaerobic hyperthermophilic eubacterium Thermotoga maritima: involvement of the Embden-Meyerhof pathway (1994)
    Springer
    Archives of microbiology 161 (1994), S. 460-470 
    Details
    ISSN: 1432-072X
    Keywords: Thermotoga maritima ; Hyperthermophiles ; (Eu)Bacteria ; Glucose fermentation ; Acetate formation ; Embden-Meyerhof pathway ; Hexokinase ; Phosphofructokinase ; Acetake kinase ; Sulfur reduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The hyperthermophilic anaerobic eubacterium Thermotoga maritima was grown on glucose as carbon and energy source. During growth 1 mol glucose was fermented to 2 mol acetate, 2 mol CO2 and 4 mol H2. The molar growth yicld on glucose (Yglucose) was about 45 g cell dry mass/mol glucose. In the presence of elemental sulfur growing cultures of T. maritima converted 1 mol glucose to 2 mol acetate, 2 mol CO2 about 0.5 mol H2 and about 3.5 mol H2S. Yglucose was about 45 g/mol. Cell extracts contained all enzymes of the Embden-Meyerhof pathway: hexokinase (0.29 U/mg, 50°C), glucose-6-phosphate isomerase (0.56 U/mg, 50°C), phosphofructokinase (0.19 U/mg, 50° C), fructose-1,6-bisphosphate aldolase (0.033 U/mg, 50°C), triosephosphate isomerase (6.3 U/mg, 50°C), glyceraldehyde-3-phosphate dehydrogenase (NAD+ reducing: 0.63 U/mg, 50°C), phosphoglycerate kinase (3.7 U/mg, 50°C), phosphoglycerate mutase (0.4 U/mg, 50°C); enolase (4 U/mg, 80°C), pyruvate kinase (0.05 U/mg, 50°C). Furthermore, cell extracts contained pyruvate: ferredoxin oxidoreductasee (0.43 U/mg, 60°C); NADH: ferredoxin oxidoreductase (benzylviologen reduction: 0.46 U/mg, 80°C); hydrogenase (benzylviologen reduction: 15 U/mg, 80°C), phosphate acetyltransferase (0.13 U/mg, 80°C), acetate kinase (1.2 U/mg, 55°C), lactate dehydrogenase (0.16 U/mg, 80°C) and pyruvate carboxylase (0.02 U/mg, 50°C). The findings indicate that the hyperthermophilic eubacterium T. maritima ferments sugars (glucose) to acetate, CO2 and H2 involving the Embden-Meyerhof pathway, phosphate acetyltransferase and acetate kinase. Thus, the organism differs from the hyperthermophilic archaeon Pyrococcus furiosus which ferments sugars to acetate, CO2 and H2 involving a modified non-phosphorylated Entner-Doudoroff pathway and acetyl-CoA synthetase (ADP forming).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307766
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  • 4
    Electronic Resource
    Electronic Resource
    Acetyl-CoA synthetase (ADP forming) in archaea, a novel enzyme involved in acetate formation and ATP synthesis (1993)
    Springer
    Archives of microbiology 159 (1993), S. 72-83 
    Details
    ISSN: 1432-072X
    Keywords: Archaea ; Bacteria ; Hyperthermophiles ; Acetate formation ; Pyruvate: ferredoxin oxidoreductase ; Acetyl-CoA synthetase (ADP forming) ; Phosphate acetyltransferase ; Acetate kinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The anaerobic hyperthermophilic archaea Desulfurococcus amylolyticus, Hyperthermus butylicus, Thermococcus celer, Pyrococcus woesei, the hyperthermophilic bacteria Thermotoga maritima and Clostridium thermohydrosulfuricum and the aerobic mesophilic archaeon Halobacterium saccharovorum were grown either on complex media, on sugars or on pyruvate as carbon and energy sources. During growth acetate was formed as fermentation product by all organisms. The enzymes involved in acetyl-CoA formation from pyruvate and in acetate formation from acetyl-CoA were investigated: 1. Cell extracts of all species, both archaea and bacteria, catalyzed the coenzyme A-dependent oxidative decarboxylation of pyruvate with viologen dyes or with Clostridium pasteurianum ferredoxin as electron acceptors indicating a pyruvate: ferredoxin oxidoreductase to be operative in acetyl-CoA formation from pyruvate. 2. Cell extracts of all archaeal species, both hyperthermophiles (D. amylolyticus, H. butylicus, T. celer, P. woesei) and the mesophile H. saccharovorum, contained an acetyl-CoA synthetase (ADP forming), which catalyzes both acetate formation from acetyl-CoA and ATP synthesis from ADP and phosphate (Pi): Acetyl-CoA+ADP+Pi⇌Acetate + ATP+CoA. Phosphate acetyltransferase and acetate kinase could not be detected. 3. Cell extracts of the hyperthermophilic (eu)bacteria T. maritima and C. thermohydrosulfuricum contained phosphate acetyltransferase and acetate kinase rather than acetyl-CoA synthetase (ADP forming). These data indicate that acetyl-CoA synthetase (ADP forming) represents a typical archaeal property rather than an enzyme specific for hyperthermophiles. It is proposed that in all acetate forming archaea the formation of acetate and of ATP from acetyl-CoA, ADP and Pi are catalyzed by acetyl-CoA synthetase (ADP forming), whereas in all acetate forming (eu)bacteria these reactions are catalyzed by two enzymes, phosphate acetyltransferase and acetate kinase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00244267
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