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  • Phenol  (3)
  • Key wordsThauera  (2)
  • Methanobacterium thermoautotrophicum  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 251 (1989), S. 237-240 
    ISSN: 0014-5793
    Keywords: (Pseudomonas) ; Anaerobic degradation ; Aromatic compound ; Benzoyl-CoA:(acceptor) 4-oxidoreductase (hydroxylating) ; Hydroxybenzoyl-CoA, 4- ; Phenol
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 136 (1983), S. 160-162 
    ISSN: 1432-072X
    Keywords: Methanobacterium thermoautotrophicum ; Aldolase ; Fructose 1,6-bisphosphatase ; Autotrophic ; Methanogen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In Methanobacterium thermoautotrophicum fructose 1,6-bisphosphate aldolase and fructose 1,6-bisphosphate phosphatase were studied, which could not be detected in previous investigations. Aldolase appeared to be a class I enzyme. Enzyme activity was only detectable in direction of aldol condensation in presence of Mg2+ and under anaerobic conditions. It was stimulated by dithioerythritol. The regulatory properties of the hexose bisphosphate phosphatase differed in many ways from those of the enzyme from other organisms.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-072X
    Keywords: Key wordsThauera ; Toluene ; Benzyl alcohol ; Toluene-oxidizing enzyme system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Toluene and related aromatic compounds can be mineralized to CO2 under anoxic conditions. Oxidation requires new dehydrogenase-type enzymes and water as oxygen source, as opposed to the aerobic enzymatic attack by oxygenases, which depends on molecular oxygen. We studied the anaerobic process in the denitrifying bacterium Thauera sp. strain K172. Toluene and a number of its fluoro-, chloro- and methyl-analogues were transformed to benzoate and the respective analogues by whole cells and by cell extracts. The transformation of xylene isomers to methylbenzoate isomers suggests that xylene degradation is similarly initiated by oxidation of one of the methyl groups. Toluene oxidation was strongly, but reversibly inhibited by benzyl alcohol. The in vitro oxidation of the methyl group was coupled to the reduction of nitrate, required glycerol for activity, and was inhibited by oxygen. Cells also contained benzyl alcohol dehydrogenase (NAD+), benzaldehyde dehydrogenase (NADP+), benzoate-CoA ligase (AMP-forming), and benzoyl-CoA reductase (dearomatizing). The toluene-oxidizing activity was induced when cells were grown anaerobically with toluene and also with benzyl alcohol or benzaldehyde, suggesting that benzyl alcohol or benzaldehyde acts as inducer. The other enzymes were similarly active in cells grown with toluene, benzyl alcohol, benzaldehyde, or benzoate. This is the first in vitro study of anaerobic oxidation of an aromatic hydrocarbon and of the whole-cell regulation of the toluene-oxidizing enzyme.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-072X
    Keywords: Key wordsThauera ; Toluene ; Benzyl alcohol ; Benzyl alcohol dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Toluene and related aromatic compounds are anaerobically degraded by the denitrifying bacterium Thauera sp. strain K172 via oxidation to benzoyl-CoA. The postulated initial step is methylhydroxylation of toluene to benzyl alcohol, which is either a free or enzyme-bound intermediate. Cells grown with toluene or benzyl alcohol contained benzyl alcohol dehydrogenase, which is possibly the second enzyme in the proposed pathway. The enzyme was purified from benzyl-alcohol-grown cells and characterized. It has many properties in common with benzyl alcohol dehydrogenase from Acinetobacter and Pseudo-monas species. The enzyme was active as a homotetramer of 160 kDa, with subunits of 40 kDa. It was NAD+-specific, had an alkaline pH optimum, and was inhibited by thiol-blocking agents. No evidence for a bound cofactor was obtained. Various benzyl alcohol analogues served as substrates, whereas non-aromatic alcohols were not oxidized. The N-terminal amino acid sequence indicates that the enzyme belongs to the class of long-chain Zn2+-dependent alcohol dehydrogenases, although it appears not to contain a metal ion that can be removed by complexing agents.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 120 (1979), S. 135-139 
    ISSN: 1432-072X
    Keywords: Carbon isotope discrimination ; Autotrophic CO2 fixation ; Methane formation ; Methanobacterium thermoautotrophicum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The fractionation of carbon isotopes by Methanobacterium thermoautotrophicum was studied during growth of the bacterium on H2 plus CO2 as sole carbon and energy sources. A 80% H2/20% CO2 gas mixture was continuously bubbled through the culture. At high gassing rates, in the absence of a “closed system effect”, cells and methane were found to be depleted in 13C relative to CO2 in the gas mixture by 2.4% and 3.4%, respectively. At low gassing rates, when more than 90% of the CO2 was converted to methane, the cells were enriched in 13C by 1.3% and methane was depleted in 13C by 0.5%; residual CO2 was enriched in 13C by 3.4%. The magnitude of isotope fractionation suggests that CO2 rather than bicarbonate is the active species of CO2 mainly utilized in both CO2 assimilation and CO2 reduction to methane. The apparent positive 13C-discrimination in cell carbon synthesis, which was observed at low gassing rates, indicates that most of the CO2 assimilated into cell material is not incorporated via reactions involved in CO2 reduction to methane.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 152 (1989), S. 273-279 
    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
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 148 (1987), S. 213-217 
    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
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