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  • 1
    Monograph available for loan
    Monograph available for loan
    Allgemeine Mikrobiologie : 53 Tabellen (2007)
    Stuttgart [u.a.] : Thieme
    Details Availability
    Call number: M 11.0304
    Type of Medium: Monograph available for loan
    Pages: XX, 678 S.
    Edition: 8., vollst. überarb. und erw. Aufl.
    ISBN: 9783134446081
    Location: Upper compact magazine
    Branch Library: GFZ Library
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  • 2
    Electronic Resource
    Electronic Resource
    Quantitative determination of 4-methylimidazole as 1-acetyl derivative in caramel color by gas-liquid chromatography (1975)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 23 (1975), S. 120-122 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60197a013
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  • 3
    Electronic Resource
    Electronic Resource
    Hydroxybenzoyl-CoA reductase: coupling kinetics and electrochemistry to derive enzyme mechanisms (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 11668-11677 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00037a004
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  • 4
    Electronic Resource
    Electronic Resource
    Evidence for an incomplete reductive carboxylic acid cycle in Methanobacterium thermoautotrophicum (1978)
    Springer
    Archives of microbiology 118 (1978), S. 121-125 
    Details
    ISSN: 1432-072X
    Keywords: Methanobacterium thermoautotrophicum ; Autotrophic CO2 fixation ; Reductive carboxylic acid cycle ; α-ketoglutarate synthase ; Amino acid synthesis ; Carboxylation reactions ; Succinate incorporation ; Citrate lyase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The involvement of reactions of the tricarboxylic acid cycle in autotrophic CO2 fixation in Methanobacterium thermoautotrophicum was investigated. The incorporation of succinate into glutamate (=α-ketoglutarate), aspartate (=oxaloacetate) and alanine (=pyruvate) was studied. The organism was grown on H2 plus CO2 at pH 6.5 in the presence of 1 mM [U-14C-]succinate. Significant amounts of the dicarboxylic acid were incorporated into cellular material under these conditions. Alanine, aspartate, and glutamate were isolated and their specific radioactivities were determined. Only glutamate was found to be labelled. Degradation of glutamate revealed that C-1 of glutamate was derived from CO2 and C-2-C-5 from succinate indicating that in M. thermoautotrophicum α-ketoglutarate is synthesized via reductive carboxylation of succinyl CoA. The finding that succinate was not incorporated into alanine and aspartate excludes that oxaloacetate and pyruvate are synthesized from α-ketoglutarate via isocitrate or citrate. This is taken as evidence that a complete reductive carboxylic acid cycle is not involved here in autotrophic CO2 fixation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00406084
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  • 5
    Electronic Resource
    Electronic Resource
    Autotrophic CO2 fixation in Acetobacterium woodii (1983)
    Springer
    Archives of microbiology 135 (1983), S. 68-73 
    Details
    ISSN: 1432-072X
    Keywords: Acetobacterium woodii ; Autotrophic CO2 fixation ; Pyruvate synthase ; Pyruvate phosphate dikinase ; Phosphoenolpyruvate carboxytransphosphorylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Earlier labeling experiments have shown that autotrophically grown Acetobacterium woodii assimilates cell carbon via direct acetyl CoA formation from 2 CO2, rather than via the Calvin cycle. Cell extracts contained the enzymes required for biosynthesis starting from acetyl CoA and CO2. Notably, pyruvate synthase, pyruvate phosphate dikinase, and phosphoenolpyruvate carboxytransphosphorylase were present in sufficiently high activities. Ribulose-1,5-bisphosphate carboxylase activity could not be detected. The observed enzyme pattern was consistent with the postulated biosynthetic pathway as deduced from 14C-labeling experiments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00419485
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  • 6
    Electronic Resource
    Electronic Resource
    Autotrophic synthesis of activated acetic acid from two CO2 inMethanobacterium thermoautotrophicum (1984)
    Springer
    Archives of microbiology 139 (1984), S. 14-20 
    Details
    ISSN: 1432-072X
    Keywords: Activated acetic acid pathway ; Methanobacterium thermoautotrophicum ; Carbon monoxide dehydrogenase ; Autotrophic CO2 fixation ; Pterin ; Archaebacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Autotrophic CO2 fixation byMethanobacterium thermoautotrophicum proceeds via a total synthesis of activated acetic acid. The origins of the individual carbon atoms were studied in vitro and in vivo. The experiments described showed: (1) Two different routes of CO2 reduction lead to the individual carbon positions in acetate. (2) The carboxyl carbon is provided by a cyanide-sensitive enzyme which reduces CO2 to a bound intermediate with the oxidation state of CO. This intermediate can be supplied by gaseous CO rather than by formate, when its synthesis from CO2 is blocked by cyanide. The characteristics of the enzymic reaction are those of carbon monoxide dehydrogenase. (3) The methyl carbon is derived from CO2 via a different cyanide-insensitive CO2 reduction path, which probably shares the initial intermediates of methanogenesis from CO2 and H2. It does not involve methyl coenzyme M. It is concluded that the pathway of autotrophic CO2 assimilation into activated acetic acid inMethanobacterium is mechanistically related to the clostridial total acetate synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00692705
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  • 7
    Electronic Resource
    Electronic Resource
    Autotrophic synthesis of activated acetic acid from two CO2 in Methanobacterium thermoautotrophicum (1985)
    Springer
    Archives of microbiology 141 (1985), S. 229-238 
    Details
    ISSN: 1432-072X
    Keywords: Methanobacterium thermoautotrophicum ; Methanopterin ; Corrinoid ; Autotrophic ; Acetyl CoA ; Methane ; Propyl iodide ; Methyl iodide ; Serine ; Vitamin B12 ; Archaebacteria ; CO2 fixation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In a previous study with Methanobacterium thermoautotrophicum evidence was presented that methanogenesis and autotrophic synthesis of activated acetic acid from CO2 are linked processes. In this study one-carbon metabolism was investigated with growing cultures and in vitro. Serine was shown to be converted into glycine and activated formaldehyde, but only traces of label from [14C-3] of serine appeared in biosynthetic one-carbon positions. This seeming discrepancy could be explained if the same activated formaldehyde is an intermediate in biosynthesis and in methanogenesis from CO2. This hypothesis was supported by demonstrating that [14C-3] of serine and [14C] formaldehyde were rapidly converted into methane, but a small portion of the label was also specifically incorporated into the methyl group of acetate. Methane and acetate synthesis in vitro were similarly stimulated by various compounds. These experiments indicate that the methyl of acetate and methane share common one-carbon precursor(s), i.e. methylene tetrahydromethanopterin, which can also be formed enzymatically from C-3 of serine or chemically from formaldehyde. Propyl iodide 20–40 μM) and methyl iodide (1–3 μM) completely inhibited growth in the dark. This effect was abolished by light. Methane formation was hardly affected. When 14CH3I was applied at an only slightly inhibitory concentration, 14C was incorporated into the methyl of acetate. In vitro, similar effects on [14C] acetate formation from 14CO2 or from [14C-3] of serine were observed, except that methyl iodide did not inhibit, but even stimulated acetate synthesis. These experiments indicate that a corrinoid is involved in acetate synthesis and probably not in methanogenesis from CO2; the metal is light-reversibly alkylated and functions in methyl transfer to the acetate methyl.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408064
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  • 8
    Electronic Resource
    Electronic Resource
    Purification and properties of benzyl alcohol dehydrogenase from a denitrifying Thauera sp. (1995)
    Springer
    Archives of microbiology 163 (1995), S. 418-423 
    Details
    ISSN: 1432-072X
    Keywords: Thauera ; 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 Pseudomonas species. The enzyme was active as a homotetramer of 160kDa, with subunits of 40kDa. 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
    URL: http://dx.doi.org/10.1007/BF00272130
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  • 9
    Electronic Resource
    Electronic Resource
    Oxidative and reductive acetyl CoA/carbon monoxide dehydrogenase pathway in Desulfobacterium autotrophicum (1988)
    Springer
    Archives of microbiology 151 (1988), S. 77-83 
    Details
    ISSN: 1432-072X
    Keywords: Desulfobacterium autotrophicum ; Tetrahydrofolate ; Formyl-tetrahydrofolate synthetase ; Pterin ; Acetyl CoA pathway ; Autotrophic ; Sulfate reducing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In Desulfobacterium autotrophicum, a facultatively autotrophic, sulfate reducing eubacterium, CO2-fixing enzymes of the acetyl CoA/CO dehydrogenase pathway but neither key enzymes of the Calvin cycle nor those of the reductive citric acid cycle were detectable. This finding substantiates the proposal that the former pathway is operating in the reductive direction for CO2 fixation into acetyl CoA, and in the oxidative direction for acetyl CoA oxidation to CO2. However, the specific activity of an essential one-carbon metabolizing enzyme of this pathway, formyl-tetrahydrofolate synthetase, was unsufficient (0.01 μmol·min-1 ·mg-1), and its apparent K m-value for l-tetrahydrofolate (10 mM) was inadequate. It is shown that the physiological cosubstrate in this bacterium is not tetrahydrofolic acid, but a tetrahydropterin containing 4 mol of l-glutamate per mol of pterin. With this coenzyme the specific formyltetrahydropterin synthetase activity (1.7 μmol·min-1·mg-1) was 170-fold higher and the apparent K m for the tetrahydropterin (0.07 mM) was 140-fold lower. This indicates that it may be essential to reexamine the enzymes of acetyl CoA/CO dehydrogenase pathway in this organism and others with the proper cellular cosubstrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00444673
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  • 10
    Electronic Resource
    Electronic Resource
    Differential induction of enzymes involved in anaerobic metabolism of aromatic compounds in the denitrifying bacterium Thauera aromatica (1998)
    Springer
    Archives of microbiology 170 (1998), S. 120-131 
    Details
    ISSN: 1432-072X
    Keywords: Key words Anaerobic aromatic metabolism ; Benzoyl-CoA reductase ; Phenylphosphate carboxylase ; 4-Hydroxybenzoyl-CoA reductase ; 2-Aminobenzoate ; Phenylalanine ; Phenylacetyl-CoA ; Phenylglyoxylate ; Toluene ; CoA ligase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Differential induction of enzymes involved in anaerobic metabolism of aromatic substrates was studied in the denitrifying bacterium Thauera aromatica. This metabolism is divided into (1) peripheral reactions transforming the aromatic growth substrates to the common intermediate benzoyl-CoA, (2) the central benzoyl-CoA pathway comprising ring-reduction of benzoyl-CoA and subsequent β-oxidation to 3-hydroxypimelyl-CoA, and (3) the pathway of β-oxidation of 3-hydroxypimelyl-CoA to three acetyl-CoA and CO2. Regulation was studied by three methods. 1. Determination of protein patterns of cells grown on different substrates. This revealed several strongly substrate-induced polypeptides that were missing in cells grown on benzoate or other intermediates of the respective metabolic pathways. 2. Measurement of activities of known enzymes involved in this metabolism in cells grown on different substrates. The enzyme pattern found is consistent with the regulatory pattern deduced from simultaneous adaptation of cells to utilisation of other aromatic substrates. 3. Immunological detection of catabolic enzymes in cells grown on different substrates. Benzoate-CoA ligase and 4-hydroxybenzoate-CoA ligase were detected only in cells yielding the respective enzyme activity. However, presence of the subunits of benzoyl-CoA reductase and 4-hydroxybenzoyl-CoA reductase was also recorded in some cell batches lacking enzyme activity. This possibly indicates an additional level of regulation on protein level for these two reductases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050623
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