ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Articles  (15)
  • Methanosarcina barkeri  (11)
  • Growth yields  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Kinetic mechanism for the ability of sulfate reducers to out-compete methanogens for acetate (1982)
    Springer
    Archives of microbiology 132 (1982), S. 285-288 
    Details
    ISSN: 1432-072X
    Keywords: Desulfobacter postgatei ; Methanosarcina barkeri ; K s values for acetate ; Methanogenesis ; Sulfate reduction ; Competition for acetate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Methanosarcina barkeri and Desulfobacter postgatei are ubiquitous anaerobic bacteria which grow on acetate or acetate plus sulfate, respectively, as sole energy sources. Their apparent K s values for acetate were determined and found to be approximately 0.2 mM for the sulfate-reducing bacterium and 3 mM for the methanogenic bacterium. In mixed cell suspensions of the two bacteria (adjusted to equal V max) the rate of acetate consumption by D. postgatei approached 15-fold the rate of M. barkeri at low acetate concentrations. The apparent inhibition of methanogenesis was of the same order as expected from the different K s value for acetate. Difference in substrate affinities can thus account for the inhibition of methanogenesis from acetate in sulfate-rich environments, where the acetate concentration is well below 1 mM.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00407967
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Growth yields and saturation constant of Desulfovibrio vulgaris in chemostat culture (1984)
    Springer
    Archives of microbiology 137 (1984), S. 236-240 
    Details
    ISSN: 1432-072X
    Keywords: Desulfovibrio vulgaris ; Dissimilatory sulfate reduction ; Growth yields ; Chemostat cultures ; Pyruvate metabolism ; ATP synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Desulfovibrio vulgaris (strain Marburg) was grown on H2 and sulfate as sole energy source in a chemostat limited by the sulfate supply. The biomass concentration and the sulfate concentration in the culture were determined as a function of the dilution rate. From the data a K S (saturation constant) for sulfate of 10 μM, a μmax of 0.23 h−1, and a $${\text{Y}}_{{\text{SO}}_{\text{4}} ^{2 - } }^{{\text{max}}}$$ of 13 g/mol were calculated. The organism was also grown in chemostat culture on H2 and sulfite, H2 and thiosulfate, and pyruvate (without sulfate). $${\text{Y}}_{{\text{SO}}_3 ^{2 - } }^{{\text{max}}}$$ was found to be 35 g/mol, $${\text{Y}}_{{\text{S}}_{\text{2}} {\text{O}}_{\text{3}} ^{2 - } }^{{\text{max}}}$$ 36 g/mol, and Y pyr max 10 g/mol. The growth yields are discussed with respect to ATP gains in dissimilatory sulfate reduction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414550
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Carbonic anhydrase activity in acetate grown Methanosarcina barkeri (1989)
    Springer
    Archives of microbiology 151 (1989), S. 137-142 
    Details
    ISSN: 1432-072X
    Keywords: Carbonic anhydrase ; Acetate metabolism ; Carbon monoxide dehydrogenase ; Methanosarcina barkeri ; Desulfobacter postgatei ; Desulfotomaculum acetoxidans ; Peptostreptococcus productus ; Methanococcus voltae ; Escherichia coli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414428
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Methyltetrahydromethanopterin as an intermediate in methanogenesis from acetate in Methanosarcina barkeri (1989)
    Springer
    Archives of microbiology 151 (1989), S. 459-465 
    Details
    ISSN: 1432-072X
    Keywords: Methanogenesis from acetate ; Methanopterin ; Methanofuran ; Coenzyme F420 ; Coenzyme M ; 7-Mercaptoheptanoylthreonine phosphate (=component B) ; Methanosarcina barkeri
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cell extracts (100,000×g) of acetate grown Methanosarcina barkeri (strain MS) catalyzed CH4 and CO2 formation from acetyl-CoA with specific activities of 50 nmol·min-1·mg protein-1. CH4 formation was found to be dependent on tetrahydromethanopterin (H4MPT) (apparent K M=4 μM), coenzyme M (H-S-CoM), and 7-mercaptoheptanoylthreonine phosphate (H-S-HTP=component B) rather than on methanofuran (MFR) and coenzyme F420 (F420). Methyl-H4MPT was identified as an intermediate. This compound accumulated when H-S-CoM and H-S-HTP were omitted from the assays. These and previous results indicate that methanogenesis from acetate proceeds via acetyl phosphate, acetyl-CoA, methyl-H4MPT, and CH3-S-CoM as intermediates. The disproportionation of formaldehyde to CO2 and CH4 was also studied. This reaction was shown to be dependent on H4MPT, MFR, F420, H-S-CoM, and H-S-HTP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00416607
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Two N 5, N 10-methylenetetrahydromethanopterin dehydrogenases in the extreme thermophile Methanopyrus kandleri: characterization of the coenzyme F420-dependent enzyme (1993)
    Springer
    Archives of microbiology 160 (1993), S. 186-192 
    Details
    ISSN: 1432-072X
    Keywords: Coenzyme F420 ; Tetrahydromethanopterin ; Hydrogenase ; H2-forming methylenetrahydromethanopterin dehydrogenase ; Methanobacterium thermoautotrophicum ; Methanosarcina barkeri ; Archaeoglobus fulgidus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract It was recently reported that the extreme thermophile Methanopyrus kandleri contains only a H2-forming N 5, N 10-methylenetetrahydromethanopterin dehydrogenase which uses protons as electron acceptor. We describe here the presence in this Archaeon of a second N 5,N 10-methylenetetrahydromethanopterin dehydrogenase which is coenzyme F420-dependent. This enzyme was purified and characterized. The enzyme was colourless, had an apparent molecular mass of 300 kDa, an isoelectric point of 3.7±0.2 and was composed of only one type of subunit of apparent molecular mass of 36 kDa. The enzyme activity increased to an optimum with increasing salt concentrations. Optimal salt concentrations were e.g. 2 M (NH4)2SO4, 2 M Na2HPO4, 1.5 M K2HPO4, and 2 M NaCl. In the absence of salts the enzyme exhibited almost no activity. The salts affected mainly the V max rather than the K m of the enzyme. The catalytic mechanism of the dehydrogenase was determined to be of the ternary complex type, in agreement with the finding that the enzyme lacked a chromophoric prosthetic group. In the presence of M (NH4)2SO4 the V max was 4000 U/mg (k cat=2400 s-1) and the K m for N 5,N 10-methylenetetrahydromethanopterin and for coenzyme F420 were 80 μM and 20 μM, respectively. The enzyme was relatively heat-stable and lost no activity when incubated anaerobically in 50 mM K2HPO4 at 90°C for one hour. The N-terminal amino acid sequence was found to be similar to that of the F420-dependent N 5, N 10-methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum, Methanosarcina barkeri, and Archaeoglobus fulgidus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00249123
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Primary structure and properties of the formyltransferase from the mesophilic Methanosarcina barkeri: comparison with the enzymes from thermophilic and hyperthermophilic methanogens (1996)
    Springer
    Archives of microbiology 165 (1996), S. 97-105 
    Details
    ISSN: 1432-072X
    Keywords: Key words Formyltransferase ; Formyltetrahydrofolate ; synthase ; Hyperthermophilic enzymes ; Methanogenic ; Archaea ; Methanosarcina barkeri
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The ftr gene encoding formylmethanofuran: tetrahydromethanopterin formyltransferase (Ftr) from Methanosarcina barkeri was cloned, sequenced, and functionally expressed in Escherichia coli. The overproduced enzyme was purified eightfold to apparent homogeneity, and its catalytic properties were determined. The primary structure and the hydropathic character of the formyltransferase from Methanosarcina barkeri were compared with those of the enzymes from Methanobacterium thermoautotrophicum, Methanothermus fervidus, and Methanopyrus kandleri. The amino acid sequence of the enzyme from Methanosarcina barkeri was 64%, 61%, and 59% identical to that of the enzyme from Methanobacterium thermoautotrophicum, Methanothermus fervidus, and Methanopyrus kandleri, respectively. A negative correlation between the hydrophobicity of the enzymes and both the growth temperature optimum and the intracellular salt concentration of the four organisms was observed. The hydrophobicity of amino acid composition was +21.6 for the enzyme from Methanosarcina barkeri (growth temperature optimum 37° C, intracellular salt concentration ≈ 0.3 M), +9.9 for the enzyme from Methanobacterium thermoautotrophicum (65°C, ≈ 0.7 M), –20.8 for the enzyme from Methanothermus fervidus (83° C, ≈ 1.0 M) and –31.4 for the enzyme from Methanopyrus kandleri (98° C, 〉 1.1 M). Generally, a positive correlation between hydrophobicity and thermophilicity of enzymes and a negative correlation between hydrophobicity and halophilicity of enzymes are observed. The findings therefore indicate that the hydropathic character of the formyltransferases compared is mainly determined by the intracellular salt concentration rather than by temperature. Sequence similarities between the formyltransferases from methanogens and an open reading frame from Methylobacterium extorquens AM1 are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050303
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Isolation and characterization of Desulfovibrio growing on hydrogen plus sulfate as the sole energy source (1978)
    Springer
    Archives of microbiology 116 (1978), S. 41-49 
    Details
    ISSN: 1432-072X
    Keywords: Desulfovibrio ; Chemolithotrophic growth ; H2-Oxidation ; Sulfate-reduction ; Growth yields ; Cell carbon synthesis ; Acetate assimilation ; Desulfoviridin ; Cytochrome c3
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two sulfate reducing bacteria (Madison and Marburg strains) that grew on H2 plus sulfate in a mineral salts medium that contained acetate and CO2 as sole carbon source were isolated from diverse environments. During growth in this medium 4.2 mol of H2 were consumed per mol of sulfate reduced to sulfide. Acetate was required for biosynthetic purposes only. Approximately 70% of the cell carbon synthesized was derived from acetate and 30% from CO2. Acetate was not involved in dissimilatory sulfate reduction. Growth of the bacteria on H2 plus sulfate was linear rather than exponential, and a doubling time at the beginning of linear growth of approximately 3 h was observed. The optimal growth temperature was found to be near 35° C. Cultures could be grown up to a density of 500 mg cells (dry weight) per liter. Growth yield studies demonstrated that between 4 and 5 g of cells (dry weight) were formed per mol of sulfate reduced to sulfide. The chemolithotrophically growing sulfate reducing isolates were identified as Desulfovibrio species by being obligately anaerobic, gram negative, non spore forming vibrios that contained desulfoviridin and cytochrome c3 (350–450 nmol/g protein). The organisms were found to be monopolarly and monotrichously flagellated. The abilities of the two strains to grow on electron donors other than H2 and to use electron acceptors other than sulfate differed considerably. The DNA base composition of the Madison and Marburg strains were 60 and 63.5 mol % GC, respectively. The taxonomic status of the strains was discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408732
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Growth yields and growth rates of Desulfovibrio vulgaris (Marburg) growing on hydrogen plus sulfate and hydrogen plus thiosulfate as the sole energy sources (1978)
    Springer
    Archives of microbiology 117 (1978), S. 209-214 
    Details
    ISSN: 1432-072X
    Keywords: Desulfovibrio ; Chemolithothrophic growth ; H2 oxidation ; Sulfate reduction ; Thiosulfate reduction ; Growth rates ; Growth yields ; Maintenance coefficients ; Y ATP max
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Desulfovibrio vulgaris (Marburg) was grown on H2 plus sulfate and H2 plus thiosulfate as the sole energy sources and acetate plus CO2 as the sole carbon sources. Conditions are described under which the bacteria grew exponentially. Specific growth rates (μ) and molar growth yields (Y) at different pH were determined. μ and Y were found to be strongly dependent on the pH. Highest growth rates and molar growth yields were observed for growth on H2 plus sulfate at pH 6.5 (μ=0.15h-1; Y SO 4 2- =8.3g·mol-1) and for growth on H2 plus thiosulfate at pH 6.8 (μ=0.21h-1; Y S 2O 3 2 =16.9g·mol-1). The growth yields were found to increase with increasing growth rates: plots of 1/Y versus 1/μ were linear. Via extrapolation to infinite growth rates a Y SO4 2- /max of 12.2g·mol-1 and a YS2O 3 2- /max of 33.5g·mol-1 was obtained. The growth yield data are interpred to indicate that dissimilatory sulfate reduction to sulfide is associated with a net synthesis of 1 mol of ATP and that near to 3 mol of ATP are formed during dissimilatory sulfite reduction to sulfide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00402310
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Propionate assimilation by methanogenic bacteria (1983)
    Springer
    Archives of microbiology 136 (1983), S. 106-110 
    Details
    ISSN: 1432-072X
    Keywords: Propionate assimilation ; Isoleucine biosynthesis ; Methanogenic bacteria ; Methanobacterium thermoautotrophicum ; Methanobrevibacter arboriphilus ; Methanosarcina barkeri ; 2-Methylbutyrate assimilation ; Regulation of isoleucine biosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Methanobacterium thermoautotrophicum, Methanobrevibacter arboriphilus, and Methanosarcina barkeri were found to assimilate propionate when growing on media supplemented with this volatile fatty acid. [1-14C]propionate was almost exclusively incorporated into isoleucine, only C-2 of which became labelled. Assimilation of propionate by M. thermoautotrophicum was specifically inhibited by isoleucine, by 2-methylbutyrate, and by 2-oxobutyrate, whereas there was little or no effect by leucine, valine, butyrate, and acetate. This finding indicates that propionate assimilation is under regulatory control by intermediates and/or the product of isoleucine biosynthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00404782
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Catalysis of an isotopic exchange between CO2 and the carboxyl group of acetate by Methanosarcina barkeri grown on acetate (1984)
    Springer
    Archives of microbiology 138 (1984), S. 365-370 
    Details
    ISSN: 1432-072X
    Keywords: Methanosarcina barkeri ; Methane formation from acetate ; 14CO2/acetate exchange reaction ; Cyanide inhibition of methanogenesis ; CO inhibition of methanogenesis ; H2 inhibition of methanogenesis ; Mechanism of methane formation from acetate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cell suspensions of Methanosarcina barkeri (strain Fusaro) grown on acetate were found to catalyze the formation of methane and CO2 from acetate (30–40 nmol/min·mg protein) and an isotopic exchange between the carboxyl group of acetate and 14CO2 (30–40 nmol/min·mg protein). An isotopic exchange between [14C]-formate and acetate was not observed. Cells grown on methanol mediated neither methane formation from acetate nor the exchange reactions. The data indicate that the isotopic exchange between CO2 and the carboxyl group of acetate is a partial reaction of methanogenesis from acetate. Both reactions were completely inhibited by low concentrations of cyanide (20 μM) or of hydrogen (0.5% in the gas phase). Methane formation from acetate was also completely inhibited by low concentrations of carbon monoxide (0.2% in the gas phase) whereas only significantly higher concentrations of CO had an effect on the exchange reaction. In the concentration range tested KCN, H2 and CO had no effect on methane formation from methanol or from H2 and CO2; however, cyanide (20 μM) also affected methane formation from CO. The results are discussed with respect to proposed mechanisms of methane and CO2 formation from acetate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00410905
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...