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  • 1
    Electronic Resource
    Electronic Resource
    Anaerobic degradation of phenol by pure cultures of newly isolated denitrifying pseudomonads (1987)
    Springer
    Archives of microbiology 148 (1987), S. 213-217 
    Details
    ISSN: 1432-072X
    Keywords: Anaerobic degradation ; Aromatic compounds ; Phenol ; Cresol ; 4-Hydroxybenzoate ; Denitrification ; Pseudomonas sp.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract From various oxic or anoxic habitats several strains of bacteria were isolated which in the absence of molecular oxygen oxidized phenol to CO2 with nitrate as the terminal electron acceptor. All strains grew in defined mineral salts medium; two of them were further characterized. The bacteria were facultatively anaerobic Gramnegative rods; metabolism was strictly oxidative with molecular oxygen, nitrate, or nitrite as electron acceptor. The isolates were tentatively identified as pseudomonads. Besides phenol many other benzene derivatives like cresols or aromatic acids were anaerobically oxidized in the presence of nitrate. While benzoate or 4-hydroxybenzoate was degraded both anaerobically and aerobically, phenol was oxidized under anaerobic conditions only. Reduced alicyclic compounds were not degraded. Preliminary evidence is presented that the first reaction in anaerobic phenol oxidation is phenol carboxylation to 4-hydroxybenzoate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414814
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  • 2
    Electronic Resource
    Electronic Resource
    Enzyme reactions involved in anaerobic cyclohexanol metabolism by a denitrifying Pseudomonas species (1989)
    Springer
    Archives of microbiology 152 (1989), S. 273-279 
    Details
    ISSN: 1432-072X
    Keywords: Alicyclic compounds ; Denitrification ; Cyclohexanol dehydrogenase ; Cyclohexanone dehydrogenase ; 2-Cyclohexenone hydratase ; 3-Hydroxycyclohexanone dehydrogenase ; 1,3-Cyclohexanedione hydrolase ; Phenol ; Aromatization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The enzymes involved in the anaerobic degration of cyclohexanol were searched for in a denitrifying Pseudomonas species which metabolizes this alicyclic compound to CO2 anaerobically. All postulated enzyme activities were demonstrated in vitro with sufficient specific activities. Cyclohexanol dehydrogenase catalyzes the oxidation of the substrate to cyclohexanone. Cyclohexanone dehydrogenase oxidizes cyclohexanone to 2-cyclohexenone. 2-Cyclohexenone hydratase and 3-hydroxycyclohexanone dehydrogenase convert 2-cyclohexenone via 3-hydroxycyclohexanone into 1,3-cyclohexanedione. Finally, the dione is cleaved by 1,3-cyclohexanedione hydrolase into 5-oxocaproic acid. Some kinetic and regulatory properties of these enzymes were studied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409663
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  • 3
    Electronic Resource
    Electronic Resource
    Acetate oxidation to CO2 via a citric acid cycle involving an ATP-citrate lyase: a mechanism for the synthesis of ATP via substrate level phosphorylation in Desulfobacter postgatei growing on acetate and sulfate (1987)
    Springer
    Archives of microbiology 148 (1987), S. 202-207 
    Details
    ISSN: 1432-072X
    Keywords: ATP-citrate lyase ; Citric acid cycle ; Acetate oxidation ; ATP synthesis via substrate level phosphorylation ; Sulfate-reducing bacteria ; Desulfobacter postgatei
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Desulfobacter postgatei is an acetate-oxidizing, sulfate-reducing bacterium that metabolizes acetate via the citric acid cycle. The organism has been reported to contain a si-citrate synthase (EC 4.1.3.7) which is activated by AMP and inorganic phosphate. It is show now, that the enzyme mediating citrate formation is an ATP-citrate lyase (EC 4.1.3.8) rather than a citrate synthase. Cell extracts (160,000xg supernatant) catalyzed the conversion of oxaloacetate (apparent K m=0.2 mM), acetyl-CoA (app. K m=0.1 mM), ADP (app. K m=0.06 mM) and phosphate (app. K m=0.7 mM) to citrate, CoA and ATP with a specific activity of 0.3 μmol·min-1·mg-1 protein. Per mol citrate formed 1 mol of ATP was generated. Cleavage of citrate (app. K m=0.05 mM; V max=1.2 μmol · min-1 · mg-1 protein) was dependent on ATP (app. K m=0.4 mM) and CoA (app. K m=0.05 mM) and yielded oxaloacetate, acetyl-CoA, ADP, and phosphate as products in a stoichiometry of citrate:CoA:oxaloacetate:ADP=1:1:1:1. The use of an ATP-citrate lyase in the citric acid cycle enables D. postgatei to couple the oxidation of acetate to 2 CO2 with the net synthesis of ATP via substrate level phosphorylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414812
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  • 4
    Electronic Resource
    Electronic Resource
    Carbon assimilation pathways in sulfate-reducing bacteria II. Enzymes of a reductive citric acid cycle in the autotrophic Desulfobacter hydrogenophilus (1987)
    Springer
    Archives of microbiology 148 (1987), S. 218-225 
    Details
    ISSN: 1432-072X
    Keywords: Desulfobacter hydrogenophilus ; Sulfate-reducing bacteria ; Autotrophy ; Citric acid cycle ; ATP-citrate lyase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The strict anaerobe Desulfobacter hydrogenophilus is able to grow autotrophically with CO2, H2, and sulfate as sole carbon and energy sources. The generation time at 30°C under autotrophic conditions in a pure mineral medium was 15 h, the growth yield was 8 g cell dry mass per mol sulfate reduced to H2S. Enzymes of the autotrophic CO2 assimilation pathway were investigated. Key enzymes of the Calvin cycle and of the acetyl CoA pathway could not be found. All enzymes of a reductive citric acid cycle were present at specific activities sufficient to account for the observed growth rate. Notably, an ATP-citrate lyase (1.3 μmol · min-1 · mg cell protein-1) was present both in autotrophically and in heterotrophically grown cells, which was rapidly inactivated in the absence of ATP. The data indicate that in D. hydrogenophilus a reductive citric acid cycle is operating in autotrophic CO2 fixation. Since other autotrophic sulfate reducers possess an acetyl CoA pathway for CO2 fixation, two different autotrophic pathways occur in the same physiological group.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414815
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  • 5
    Electronic Resource
    Electronic Resource
    Studies on the anaerobic degradation of benzoic acid and 2-aminobenzoic acid by a denitrifying Pseudomonas strain (1987)
    Springer
    Archives of microbiology 149 (1987), S. 62-69 
    Details
    ISSN: 1432-072X
    Keywords: Aromatic compounds ; 2-Aminobenzoic acid ; Benzoic acid ; Anaerobic degradation ; Pseudomonas sp ; Anthranilic acid ; Denitrification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The growth of a denitrifying Pseudomonas strain on benzoic acid and 2-aminobenzoic acid (anthranilic acid) has been studied. The organism grew aerobically on benzoate, 2-aminobenzoate, and gentisate, but not on catechol or protocatechuic acid. These and other findings suggest that aerobic degradation of benzoic acid was via gentisic acid. Under completely anaerobic conditions in the presence of nitrate, benzoate and 2-aminobenzoate (5 mM each) were oxidized to CO2 with the concurrent reduction of NO 3 - to NO 2 - . Only after complete NO 3 - consumption was NO 2 - reduced to N2. Cells contained a NADP-specific 2-oxoglutaate dehydrogenase, in contrast to a NAD-specific pyruvate dehydrogenase. During anaerobic metabolism of [carboxyl-14C]benzoic acid, 16% of the label of metabolized benzoic acid was incorporated into cell material; this excludes intermediary decarboxylation during anaerobic metabolism. Extracts catalysed the activation of benzoic acid and a variety of its derivatives to the respective aryl-coenzyme A thioesters, ATP being cleaved to AMP and PPi; two synthetase activites were present. Extracts from 2-aminobenzoate-grown cells catalyzed a NADH-dependent reduction of 2-aminobenzoyl-CoA (100 nmol·min-1·mg-1 cell protein) to an unidentified CoA thioester, with a stoichiometric release of NH3 and a stoichiometry of ≈ 3 mol NADH oxidized per mol 2-aminobenzyol-CoA reduced when tested under aerobic conditions. The 2-aminobenzoyl-CoA reductase activity was lacking in anaerobic benzoate-grown cells and in aerobic cells. This is taken as evidence that 2-aminobenzoyl-CoA reductase is a key enzyme in a novel reductive pathway of anaerobic 2-aminobenzoic acid metabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00423138
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