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  • Artikel  (7)
  • Carbon monoxide dehydrogenase  (7)
  • 1
    ISSN: 1432-072X
    Schlagwort(e): Desulfovibrio baarsii ; Autotroph ; Sulfate reducing bacteria ; Activated acetic acid pathway ; Formate ; Carbon monoxide dehydrogenase ; Pyruvate synthesis ; Ribulose-bisphosphate carboxylase
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Desulfovibrio baarsii is a sulfate reducing bacterium, which can grown on formate plus sulfate as sole energy source and formate and CO2 as sole carbon sources. It is shown by 14C labelling studies that more than 60% of the cell carbon is derived from CO2 and the rest from formate. The cells thus grow autotrophically. Labelling studies with [14C]acetate, 14CO and [14C]formate indicate that CO2 fixation does not proceed via the Calvin cycle. The labelling patterns of alanine, aspartate, glutamate, and glucosamine indicate that acetate (or activated acetic acid) is an early intermediate in formate and CO2 assimilation; the methyl group of acetate is derived from formate, and the carboxyl group from CO2 via CO; pyruvate is formed from acetyl-CoA by reductive carboxylation. The capacity to synthesize an acetate unit from two C1-compounds obviously distinguishes D. baarsii from those Desulfovibrio species, which require acetate as a carbon source in addition to CO2.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Archives of microbiology 150 (1988), S. 374-380 
    ISSN: 1432-072X
    Schlagwort(e): Desulfotomaculum ; Sulfate reduction ; Acetate oxidation ; Acetyl-CoA ; Carbon monoxide dehydrogenase ; Tetrahydrofolates ; Acetyl-CoA/carbon monoxide dehydrogenase pathway ; Citric acid cycle
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Desulfotomaculum acetoxidans has been proposed to oxidize acetate to CO2 via an oxidative acetyl-CoA/carbon monoxide dehydrogenase pathway rather than via the citric acid cycle. We report here the presence of the enzyme activities required for the operation of the novel pathway. In cell extracts the following activities were found (values in brackets=specific activities and apparent K m; 1 U·mg-1=1 μmol·min-1·mg protein-1 at 37°C): Acetate kinase (6.3 U·mg-1; 2 mM acetate; 2.4 mM ATP); phosphate acetyltransferase (60 U·mg-1, 0.4 mM acetylphosphate; 0.1 mM CoA); carbon monoxide dehydrogenase (29 U·mg-1; 13% carbon monoxide; 1.3 mM methyl viologen); 5,10-methylenetetrahydrofolate reductase (3 U·mg-1, 0.06 mM CH3−FH4); methylenetetrahydrofolate dehydrogenase (3.6 U·mg-1, 0.9 mM NAD, 0.1 mM CH2=FH4); methenyltetrahydrofolate cyclohydrolase (0.3 U·mg-1); formyltetrahydrofolate synthetase (3 U·mg-1, 1.4 mM FH4, 0.4 mM ATP, 13 mM formate); and formate dehydrogenase (10 U·mg-1, 0.4 mM formate, 0.5 mM NAD). The specific activities are sufficient to account for the in vivo acetate oxidation rate of 0.26 U·mg-1.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Springer
    Archives of microbiology 151 (1989), S. 137-142 
    ISSN: 1432-072X
    Schlagwort(e): Carbonic anhydrase ; Acetate metabolism ; Carbon monoxide dehydrogenase ; Methanosarcina barkeri ; Desulfobacter postgatei ; Desulfotomaculum acetoxidans ; Peptostreptococcus productus ; Methanococcus voltae ; Escherichia coli
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Cell extracts (27000xg supernatant) of acetate grown Methanosarcina barkeri were found to have carbonic anhydrase activity (0.41 U/mg protein), which was lost upon heating or incubation with proteinase K. The activity was inhibited by Diamox (apparent K i=0.5 mM), by azide (apparent K i=1 mM), and by cyanide (apparent K i=0.02 mM). These and other properties indicate that the archaebacterium contains the enzyme carbonic anhydrase (EC 4.2.1.1). Evidence is presented that the protein is probably located in the cytoplasm. Methanol or H2/CO2 grown cells of M. barkeri showed no or only very little carbonic anhydrase activity. After transfer of these cells to acetate medium the activity was “induced” suggesting a function of this enzyme in acetate fermentation to CO2 and CH4. Interestingly, Desulfobacter postgatei and Desulfotomaculum acetoxidans, which oxidize acetate to 2 CO2 with sulfate as electron acceptor, were also found to exhibit carbonic anhydrase activity (0.2 U/mg protein).
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Springer
    Archives of microbiology 152 (1989), S. 189-195 
    ISSN: 1432-072X
    Schlagwort(e): Desulfotomaculum ; Sulfate reduction ; Acetate oxidation ; Acetyl-CoA/carbon monoxide dehydrogenase pathway ; Carbon monoxide dehydrogenase ; Carbon monoxide formation ; Electron transport phosphorylation coupled to acetate oxidation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Desulfotomaculum acetoxidans oxidizes acetate to CO2 with sulfate. This organism metabolizes acetate via a pathway in which C1 units rather than tri- and dicarboxylic acids are intermediates. We report here that cell extracts of D. acetoxidans catalyzed an exchange between CO2 and the carboxyl group of acetate at a rate of 90 nmol · min-1 · mg-1 protein which is sufficient to account for the in vivo acetate oxidation rate of 250 nmol · min-1 · mg-1 protein. The reaction was strictly dependent on both ATP and coenzyme A. The extracts contain high activities of acetate kinase (6.3 U · mg-1 protein) and phosphotransacetylase (60 U · mg-1 protein). These findings indicate that acetyl-CoA rather than acetyl-phosphate or acetate is the substrate of the carbon-carbon cleavage activity. Exchange was only observed in the presence of strong reducing agents such as Ti3+. Interestingly, the cell extracts also catalyzed the reduction of CO2 to CO with Ti3+ as electron donor (120 nmol · min-1 · mg-1 protein). Carbon monoxide dehydrogenase and other oxidoreductases involved in acetate oxidation were found to be partially associated with the membrane fraction suggesting a membrane localization of these enzymes.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
    ISSN: 1432-072X
    Schlagwort(e): Methanobrevibacter ruminantium ; Methanobrevibacter smithii ; Methanococcus voltae ; Methanospirillum hungatei ; Carbon monoxide dehydrogenase ; Carbon monoxide formation ; Carbon monoxide utilization ; Carbonylation reaction ; Autotrophic CO2 fixation ; Acetyl-CoA pathway
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Autotrophic methanogens reduce CO2 to CO and assimilate CO in a carbonylation reaction. Heterotrophic species were found not to form CO and/or to incorporate CO into cell matiral. The absence of CO formation correlated with the absence of carbon monoxide dehydrogenase activity. The heterotrophic Methanobrevibacter ruminantium, Methanobrevibacter smithii, Methanococcus voltae and Methanospirillum hungatei (strain GP 1) were investigated.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 6
    ISSN: 1432-072X
    Schlagwort(e): Methanosarcina barkeri ; Acetate metabolism ; Methanogenesis from acetate ; H2 metabolism ; Carbon monoxide dehydrogenase ; Cyanide inhibition ; Nitrous oxide inhibition
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract From our previous studies on the mechanism of methane formation from acetate it was known that cell extracts of acetate-grown Methanosarcina barkeri (100 000 × g supernatant) catalyze the conversion of acetyl-CoA plus tetrahydromethanopterin (=H4MPT) to methyl-H4MPT, CoA, CO2 and presumably H2. We report here that these extracts, in the absence of H4MPT, mediated an isotope exchange between CO2 ([S]0.5 v=0.2% in the gas phase) and the carbonyl group of acetyl-CoA at almost the same specific rate as the above conversion (10 nmol · min−1 · mg protein−1). Both the exchange and the formation of methyl-H4MPT were inhibited by N2O, suggesting that a corrinoid could be the primary methyl group acceptor in the acetyl-CoA C-C-cleavage reaction. Both activities were dependent on the presence of H2 (E0′=−414 mV). Ti(III)citrate (E0′=−480 mV) was found to substitute for H2, indicating a reductive activation of the system. In the presence of Ti(III)citrate it was shown that the formation of CO2 from the carbonyl group of acetyl-CoA is associated with a 1:1 stoichiometric generation of H2. Free CO, a possible intermediate in CO2 and H2 formation, was not detected.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 7
    ISSN: 1432-072X
    Schlagwort(e): Archaeoglobus ; Archaebacteria ; Thermophiles ; Sulfate-reducing bacteria ; Lactate oxidation ; Carbon monoxide dehydrogenase ; Acetyl-CoA decarbonylation ; C1-pathway
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Cell extracts of Archaeoglobus fulgidus were found to catalyze an isotope exchange between CO2 and the carbonyl group of acetyl-CoA. This observation and the presence of carbon monoxide: methyl viologen oxidoreductase activity strongly support the recent proposal that in A. fulgidus acetyl-CoA is degraded via a decarbonylation reaction.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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