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  • 1
    Electronic Resource
    Electronic Resource
    The dissimilatory sulfite reductase from Desulfosarcina variabilis is a desulforubidin containing uncoupled metalated sirohemes and S = 9/2 iron-sulfur clusters (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 10323-10330 
    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/bi00090a007
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  • 2
    Electronic Resource
    Electronic Resource
    A fluoride-insensitive inorganic pyrophosphatase isolated from Methanothrix soehngenii (1992)
    Springer
    Archives of microbiology 157 (1992), S. 284-289 
    Details
    ISSN: 1432-072X
    Keywords: Methanothrix soehngenii ; Acetate degradation ; Energetics ; Inorganic pyrophosphatase ; Fluoride inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An inorganic pyrophosphatase [E.C. 3.6.1.1] was isolated from Methanothrix soehngenii. In three steps the enzyme was purified 400-fold to apparent homogeneity. The molecular mass estimated by gelfiltration was 139±7 kDa. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis indicated that the enzyme is composed of subunits with molecular masses of 35 and 33 kDa in an α 2 β 2 oligomeric structure. The enzyme catalyzed the hydrolysis of inorganic pyrophosphate, tri-and tetrapolyphosphate, but no activity was observed with a variety of other phosphate esters. The cation Mg2+ was required for activity. The pH optimum was 8 at 1 mM PP i and 5 mM Mg2+. The enzyme was heat-stable, insensitive to molecular oxygen and not inhibited by fluoride. Analysis of the kinetic properties revealed an apparent K m for PP i of 0.1 mM in the presence of 5 mM Mg2+. The V max was 590 μmol of pyrophosphate hydrolyzed per min per mg protein, which corresponds to a K cat of 1400 per second. The enzyme was found in the soluble enzyme fraction after ultracentrifugation, when cells were disrupted by French Press. Upto 5% of the pyrophosphatase was associated with the membrane fraction, when gentle lysis procedyre were applied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245163
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  • 3
    Electronic Resource
    Electronic Resource
    Oxidative and reductive acetyl CoA/carbon monoxide dehydrogenase pathway in Desulfobacterium autotrophicum (1988)
    Springer
    Archives of microbiology 151 (1988), S. 84-89 
    Details
    ISSN: 1432-072X
    Keywords: Desulfobacterium autotrophicum ; Acetyl CoA pathway ; Carbon monoxide dehydrogenase ; Sulfate reducing ; Pterin ; Autotrophic ; Acetate oxidation ; Citric acid cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract It has been proposed that in some anaerobic facultatively autotrophic bacteria the acetyl CoA/CO dehydrogenase pathway is operating both in the reductive and in the oxidative direction, depending on the growth conditions. One of these anaerobes, the Gram-negative sulfate-reducing cubacterium Desulfobacterium autotrophicum, was examined for enzymes of the proposed pathway. All the required enzyme activities were present in sufficient amounts both in autotrophically and in heterotrophically grown cells, provided that the cellular tetrahydropterin rather than tetrahydrofolate was used as cosubstrate in some of the enzyme assays. The question arises whether two sets of enzymes are operating in the reductive and oxidative direction, respectively. The key enzyme of this pathway, CO dehydrogenase, which was reasonably oxygen stable, was analysed by native polyacrylamide gel electrophoresis and anaerobic activity staining. Extracts from heterotrophically grown cells exhibited five enzyme activity bands. Extracts from autotrophically grown cells showed the same pattern but an additional activity band appeared.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00444674
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  • 4
    Electronic Resource
    Electronic Resource
    Growth of Nitrosomonas europaea on hydroxylamine (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 125 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Hydroxylamine is an intermediate in the oxidation of ammonia to nitrite, but until now it has not been possible to grow Nitrosomonas europaea on hydroxylamine. This study demonstrates that cells of N. europaea are capable of growing mixotrophically on ammonia and hydroxylamine. The molar growth yield on hydroxylamine (4.74 g mol−1 at a growth rate of 0.03 h−1) was higher than expected. Aerobically growing cells of N. europaea oxidized ammonia to nitrite with little loss of inorganic nitrogen, while significant inorganic nitrogen losses occurred when cells were growing mixotrophically on ammonia and hydroxylamine. In the absence of oxygen, hydroxylamine was oxidized with nitrite as electron acceptor, while nitrous oxide was produced. Anaerobic growth of N. europaea on ammonium, hydroxylamine and nitrite could not be observed at growth rates of 0.03 h−1 and 0.01 h−1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07355.x
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  • 5
    Electronic Resource
    Electronic Resource
    Adenine nucleotide content and energy charge of Methanothrix soehngenii during acetate degradation (1991)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 84 (1991), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The interconversion of adenine nucleotides during acetate fermentation was investigated with concentrated cell suspensions of Methanothrix soehngenii. Starved cells contained high levels of AMP (2.2 nmol/mg protein), but had hardly any ADP or ATP. The energy charge of these cells was 0.1. Immediately after the addition of the substrate acetate, the level of ATP increased, reaching a maximum of 1.4 nmol/mg protein, corresponding to an energy charge of 0.7 when half of the acetate was consumed. Once the acetate was depleted, the ATP concentration decreased to its original level of 0.1 nmol/mg protein. As M. soehngenii contained relatively high amounts of AMP, the luciferase system for the determination of ATP gave not always satisfactory results. Therefore a reliable method based on the separation of adenine nucleotides by anion exchange HPLC was used.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1991.tb04616.x
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  • 6
    Electronic Resource
    Electronic Resource
    Purification and some properties of the methyl-CoM reductase of Methanothrix soehngenii (1990)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 66 (1990), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The methyl-CoM reductase from Methanothrix soehngenii was purified 18-fold to apparent homogeneity with 50% recovery in three steps. The native molecular mass of the enzyme estimated by gel-fitration was 280 kDa. SDS-polyacrylamide gel electrophoresis revealed three protein bands corresponding to Mr 63 900, 41 700 and 30 400 Da. The methyl-coenzyme M reductase constitutes up to 10% of the soluble cell protein. The enzyme has Km apparent values of 23 μM and 2 mM for N-7-mercaptoheptanoylthreonine phosphate (HS- HTP=componentB) and methyl-coenzyme M (CH3?CoM) respectively. At the optimum pH of 7.0 60 nmol of methane were formed per min per mg protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1990.tb03993.x
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of phosphoenolpyruvate carboxykinase from Corynebacterium glutamicum (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 111 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Phosphoenolpyruvate (PEP) carboxykinase is present in crude extracts of Corynebacterium glutamicum grown on both glucose and lactate. Preparation of PEP carboxykinase free from interfering PEP carboxylase and oxaloacetate decarboxylase showed an absolute dependence on divalent manganese and IDP for activity in the oxaloacetate (OAA) formation. Other diphosphate nucleotides could not substitute for IDP. The enzyme activity displayed Michaelis-Menten kinetics for the substrates PEP, IDP, KHCO3, OAA and ITP with a Km of 0.7 mM, 0.4 mM, 12 mM, 1.0 mM, and 0.5 mM, respectively. At the optimum pH of 6.6, 850 nmol of OAA were formed per min per mg of protein. ATP inhibited PEP carboxykinase in the OAA forming reaction for 60% at 0.1 mM, indicating that the enzyme mainly functions in gluconeogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06383.x
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  • 8
    Electronic Resource
    Electronic Resource
    Acetate threshold values and acetate activating enzymes in methanogenic bacteria (1990)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 73 (1990), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The minimum threshold concentrations of acetate utilization and the enzymes responsible for acetate activation of several methanogenic bacteria were investigated and compared with literature data. The minimum acetate concentrations reached by hydrogenotrophic methane bacteria, which require acetate as carbon source, were between 0.4 and 0.6 mM. The acetoclastic Methanosarcina achieves acetate concentrations between 0.2 and 1.2 mM and Methanothrix between 7 and 70 μM. For the activation of acetate most of the hydrogenotrophic methane bacteria investigated use an acetyl-CoA synthetase with a relatively low Km (40–90 μM) for acetate. although the affinity for acetate was high, the hydrogenotrophic methane bacteria were not able to remove acetate to lower concentrations than the acetoclastic methane bacteria, neither in pure cultures nor in anaerobic granular sludge samples. Based on these observations, it is not likely that hydrogenotrophic methanogens compete strongly for acetate with the acetoclastic methane bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1990.tb03958.x
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  • 9
    Electronic Resource
    Electronic Resource
    A new soluble 10 kDa monoheme cytochrome c-552 from the anammox bacterium Candidatus“Kuenenia stuttgartiensis” (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 252 (2005), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The chemolithoautotrophic anammox bacterium Candidatus“Kuenenia stuttgartiensis” grows anaerobically using ammonium as electron donor for nitrite reduction. More than 10% of the proteins in cell extracts of “K. stuttgartiensis” consist of c-type heme proteins. A 10 kDa soluble cytochrome c was purified from cell extracts using ultracentrifugation and anion exchange chromatography. The UV/Vis spectrum of the reduced cytochrome showed the γ, β and α absorption maxima at 419, 522 and 552 nm, respectively. The N-terminal amino acid sequence and peptide fragments of the tryptic digest of the protein were used to identify the corresponding gene. Analysis of the gene product showed that the protein was preceded by a 30 amino acids long leader sequence and that it belonged to the low-spin class ID cytochrome c. The CXXCH motive was located at the N-terminal site of the protein. The gene organization of the cytochrome showed some resemblance to cytochrome c clusters of unknown function in the genome of Nitrosomonas europaea and Geobacter sulfurreducens PCA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsle.2005.09.007
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  • 10
    Electronic Resource
    Electronic Resource
    Metabolic Engineering of Corynebacterium glutamicuma (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 721 (1994), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1994.tb47373.x
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