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  • ATP formation  (1)
  • Key words:Thermotoga maritima– Hyperthermophiles – (Eu)Bacteria – Glucose fermentation – Acetate formation – Embden-Meyerhof pathway – Hexokinase – Phosphofructokinase – Acetate kinase – Sulfur reduction  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Glucose fermentation of 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: Key words:Thermotoga maritima– Hyperthermophiles – (Eu)Bacteria – Glucose fermentation – Acetate formation – Embden-Meyerhof pathway – Hexokinase – Phosphofructokinase – Acetate 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 yield 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 oxidoreductase (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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  • 2
    Electronic Resource
    Electronic Resource
    ATP formation coupled to caffeate reduction by H2 in Acetobacterium woodii NZva16 (1988)
    Springer
    Archives of microbiology 150 (1988), S. 447-451 
    Details
    ISSN: 1432-072X
    Keywords: Acetobacterium woodii ; Caffeate reduction ; ATP formation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have addressed the question, whether the reduction of caffeate in Acetobacterium woodii strain NZva16 is coupled to ATP synthesis by electron transport phosphorylation. The following results were obtained: 1. Cultures of A. woodii with H2 and CO2, grew to greater cell densities, when caffeate was also present. Caffeate was reduced to give hydrocaffeate and less acetate was formed. The cell yield based on the amount of caffeate reduced was approximately 1 g dry cells/mol. 2. Non-growing bacterial suspensions catalyzed the reduction of caffeate by H2. The specific activity (0.2–1.0 μmol · min−1 · mg−1 bacterial protein) was as high as expected for a catabolic reaction. 3. The ATP content of bacteria incubated, with H2 increased from 〈 1 to about 7 μmol per g cellular protein on the addition of caffeate. The ATP yield was calculated as 0.06 mol ATP · mol−1 caffeate from the initial velocity of ATP formation and the activity of caffeate reduction. Valinomycin together with nigericin inhibited ATP formation and caused a 2–3-fold increase of the activity of caffeate reduction. Protonophores were without, effect. 4. Caffeate in the presence of H2 caused the uptake of tetraphenylphosphonium cation by the bacteria. The uptake was abolished by valinomycin plus nigericin, and was considerably enhanced by monensin. Protonophores were without effect, even in the presence of monensin. It is concluded that caffeate reduction by H2 is coupled to ATP formation by electron transport phosphorylation. However, the failure of protonophores to prevent phosphorylation and TPP uptake cannot be explained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00422285
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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