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  • 11
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 9 (1980), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 12
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 20 (1983), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract ATP synthesis driven by a potassium diffusion potential was studied in cell suspensions of Methanobacterium thermoautotrophicum (Marburg). This transient increase in the intracellular ATP content was stimulated five-fold by the addition of sodium ions, from about 2 nmol ATP/min × mg cells (dry weight) at 0.07 mM Na+ to about 10 nmol ATP/min × mg cells at 25 mM Na+.
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  • 13
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 250 (2005), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The Escherichia coli strain Pgi-UdhA, a mutant of the strain MG1655, is deficient in both the pgi gene and the udhA gene and cannot grow on glucose as carbon and energy source. This strain was transformed with different pET-plasmids containing archaeal or bacterial pgi, cpgi or pgi/pmi genes from the three known PGI families (PGI, PGI/PMI, cPGI). Growth could be restored upon plasmid-based expression of pgi, pgi/pmi or cpgi genes indicating that these heterologous proteins can substitute for E. coli PGI. However, complete restoration of the growth rate could not be obtained by any of the PGIs, PGI/PMIs, or cPGIs used. The data indicate that the PGI function of the three PGI families is functionally exchangeable in glycolysis.
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  • 14
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 57 (1989), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Washed cells of Peptostreptococcus productus (strain Marburg), which were incubated in the presence of CO/CO2/N2 (50%/ 17%/ 33%; 200 kPa) catalyzed the synthesis of acetate from carbon monoxide. The rate of acetate formation from CO was stimulated more than threefold by the addition of sodium (10 mM); potassium did not effect acetate synthesis. The degree of stimulation was dependent on the sodium concentration; the dependence followed simple Michaelis-Menten kinetics. The apparent Km for sodium was determined to be about 2 mmol/1. Sodium also stimulated acetate synthesis from H2 plus CO2. In the absence of added sodium the formation of formate as an intermediate in methyl group synthesis was stimulated. It is suggested that the sodium dependent reaction(s) is one (or more) of the reactions involved in methyl group synthesis from CO2.
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  • 15
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 12 (1981), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 16
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 120 (1979), S. 73-76 
    ISSN: 1432-072X
    Keywords: Ferredoxin ; Clostridium pasteurianum ; Pyruvate synthase ; Iron-sulfur proteins ; Iron metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Clostridium pasteurianum was grown in batch cultures on media with an initial iron concentration of 10 μM. The uptake of iron and the synthesis of ferredoxin was followed. All the iron present in the medium was taken up by the cells before 50% of the final cell density was attained. The bacteria then continued to grow in the complete absence of exogenous iron. Ferredoxin was synthesized during growth until the exogenous iron concentration dropped below 1 μM. During growth in the absence of iron ferredoxin was degraded with the result that at the end of growth the cells did not contain ferredoxin. The specific activity of the iron sulfur protein, pyruvate synthase (E.C. 1.2.7.1), remained constant during growth of C. pasteurianum in the absence of exogenous iron. This finding suggests that ferredoxin was used as an endogenous source of iron for the synthesis of essential iron proteins during periods of iron deprivation.
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  • 17
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 123 (1979), S. 105-107 
    ISSN: 1432-072X
    Keywords: Nickel ; Cobalt ; Molybdenum ; Iron ; Methanobacterium thermoautotrophicum ; Trace elements
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Growth of Methanobacterium thermoautotrophicum on H2 and CO2 as sole energy and carbon sources was found to be dependent on Ni, Co, and Mo. At low concentrations of Ni (〈100 nM), Co (〈10 nM) and Mo (〈10 nM) the amount of cells formed was roughly proportional to the amount of transition metal added to the medium; for the formation of 1 g cells (dry weight) approximately 150 nmol NiCl2, 20 nmol CoCl2 and 20 nmol Na2MoO4 were required. A dependence of growth on Cu, Mn, Zn, Ca, Al, and B could not be demonstrated. Conditions are described under which the bacterium grew exponentially with a doubling time of 1.8 h up to a cell density of 2 g cells (dry weight)/1.
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  • 18
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 136 (1983), S. 69-73 
    ISSN: 1432-072X
    Keywords: Desulfovibrio vulgaris ; Sodium transport ; Na+/H+ antiport ; Dissimilatory sulfate reduction ; Sulfate transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Entry of sodium ions into cells of Desulfovibrio vulgaris was studied. Translocation of Na+ was monitored by following the optical changes associated with shrinkage and swelling of the cells upon exposure to a hyperosmotic solution (200 mM) of sodium acetate or of sodium thiocyanate. By this technique the two solutes were found to equilibrate only after the addition of a protonophore such as carbonylcyanide m-chlorophenyl-hydrazone (CCCP). It was confirmed that acetate permeates electroneutrally as CH3COOH and thiocyanate electrogenically as SCN-. These findings suggest that Na+ is translocated by an electrogenic sodium ion/hydrogen ion antiport mechanism (H+/Na+〉1). Consistent with this interpretation is the observation that the addition of sodium acetate to a cell suspension resulted in the generation of a membrane potential (inside negative) and that of NaCl in an acidification of the external medium.
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  • 19
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 137 (1984), S. 362-365 
    ISSN: 1432-072X
    Keywords: Coenzyme F420 ; Flavin biosynthesis ; Deazaflavins ; Guanine assimilation ; Methanogenic bacteria ; Methanobacterium thermoautotrophicum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Coenzyme F420 is a 8-hydroxy-5-deazaflavin present in methanogenic bacteria. We have investigated whether the pyrimidine ring of the deazaflavin originates from guanine as in flavin biosynthesis, in which the pyrimidine ring of guanine is conserved. For this purpose the incorporation of [2-14C]guanine and of [8-14C]guanine into F420 by growing cultures of Methanobacterium thermoautotrophicum was studied. Only in the case of [2-14C]guanine did F420 become labeled. The specific radioactivity of the deazaflavin and of guanine isolated from nucleic acids of [2-14C]guanine grown cells were identical. This finding suggests that the pyrimidine ring of the deazaflavin and of flavins are synthesized by the same pathway. F420 did not become labeled when M. thermoautotrophicum was grown in the presence of methyl-[14C] methionine, [U-14C]phenylalanine or [U-14C]tyrosine. This excludes that C-5 of the deazaflavin is derived from the methyl group of methionine and that the benzene ring comes from phenylalanine or tyrosine.
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  • 20
    ISSN: 1432-072X
    Keywords: Pyrococcus furiosus ; Archaea ; Hyperthermophiles ; Gluconeogenesis ; Embden-Meyerhof pathway ; Fructose-1,6-bisphosphate aldolase ; Fructose-1,6-bisphosphate phosphatase ; Glyceraldehyde-3-phosphate dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The hyperthermophilic archaeon Pyrococcus furiosus was grown on pyruvate as carbon and energy source. The enzymes involved in gluconeogenesis were investigated. The following findings indicate that glucose-6-phosphate formation from pyruvate involves phosphoenolpyruvate synthetase, enzymes of the Embden-Meyerhof pathway and fructose-1,6-bisphosphate phosphatase. Cell extracts of pyruvate-grown P.furiosus contained the following enzyme activities: phosphoenolpyruvate synthetase (0.025 U/mg, 50 °C), enolase (0.9 U/mg, 80 °C), phosphoglycerate mutase (0.13 U/mg, 55 °C), phosphoglycerate kinase (0.01 U/mg, 50 °C), glyceraldehyde-3-phosphate dehydrogenase reducing either NADP+ or NAD+ (NADP+: 0.019 U/mg, NAD+: 0.009 U/mg; 50 °C), triosephosphate isomerase (1.4 U/mg, 50 °C), fructose-1,6-bisphosphate aldolase (0.0045 U/mg, 55 °C), fructose-1,6-bisphosphate phosphatase (0.026 U/mg, 75 °C), and glucose-6-phosphate isomerase (0.22 U/mg, 50 °C). Kinetic properties (V max values and apparent K m values) of the enzymes indicate that they operate in the direction of sugar synthesis. The specific enzyme activities of phosphoglycerate kinase, glyceraldehyde-3-phosphate dehydrogenase (NADP+-reducing) and fructose-1,6-bisphosphate phosphatase in pyruvate-grown P. furiosus were by a factor of 3, 10 and 4, respectively, higher as compared to maltose-grown cells suggesting that these enzymes are induced under conditions of gluconeogenesis. Furthermore, cell extracts contained ferredoxin: NADP+ oxidoreductase (0.023 U/mg, 60 °C); phosphoenolpyruvate carboxylase (0.018 U/mg, 50 °C) acts as an anaplerotic enzyme. Thus, in P. furiosus sugar formation from pyruvate involves reactions of the Embden-Meyerhof pathway, whereas sugar degradation to pyruvate proceeds via a modified “non-phosphorylated” Entner-Doudoroff pathway.
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