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  • 1
    Electronic Resource
    Electronic Resource
    Selection of sulphur sources for the growth of Butyribacterium methylotrophicum and Acetobacterium woodii (1989)
    Springer
    Applied microbiology and biotechnology 32 (1989), S. 186-192 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Sulphide and cysteine inhibited growth of batch cultures of Butyribacterium methylotrophicum at moderate concentrations (above 0.5 mM) during growth on glucose (10 mM). The ability of several sulphur sources to replace sulphide was tested in cultures of B. methylotrophicum or Acetobacterium woodii. With sulphite (1 mM), thiosulphate (0.5 mM), elemental sulphur, and dithionite (1 mM), but not sulphate (1 mM), cultures of both organisms grew and produced some sulphide. With elemental sulphur as the sulphur source, toxic levels of sulphide accumulated. Optimal levels for the cultivation of B. methylotrophicum with sulphite were 0.5–2.0 mM, but at higher concentrations the growth rate decreased rapidly, while with dithionite up to 4.0 mM the growth rate was relatively unaffected. In chemostat cultures of B. methylotrophicum with dithionite (1 mM) as the sulphur source and glucose as the limiting substrate, dilution rates up to 0.40 h−1 were obtained. Thiosulphate could only be used in batch cultures in combination with the reductant titanium(III)nitriloacetate, but in continuous cultures the addition of the reductant to the reservoir was not necessary, because once growth had started enough sulphide was produced to keep the fermentor reduced. The maximum growth rate of B. methylotrophicum with thiosulphate in batch and continuous culture was 0.26 h−1. Both thiosulphate and dithionite are more convenient sulphur sources than sulphide, but dithionite is more versatile because of its reductive properties and the faster growth it allows.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00165886
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  • 2
    Electronic Resource
    Electronic Resource
    Fermentation of glutamate and other compounds by Acidaminobacter hydrogenoformans gen. nov. sp. nov., an obligate anaerobe isolated from black mud. Studies with pure cultures and mixed cultures with sulfate-reducing and methanogenic bacteria (1984)
    Springer
    Archives of microbiology 137 (1984), S. 329-337 
    Details
    ISSN: 1432-072X
    Keywords: Acidaminobacter hydrogenoformans gen. nov. sp. nov. ; Glutamate degradation ; Amino acid fermentation ; Interspecies hydrogen transfer ; Syntrophic cultures ; Sulfate reduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract From mud from the Ems-Dollard estuary (The Netherlands) an L-glutamate-fermenting bacterium was isolated. The isolated strain glu 65 is Gram-negative, rodshaped, obligately anaerobic, non-sporeforming and does not contain cytochromes. The G+C content of its DNA is 48 mol percent. Pure cultures of strain glu 65 grew slowly on glutamate (μmax 0.06 h-1) and formed acetate, CO2, formate and hydrogen, and minor amounts of propionate. A more rapid fermentation of glutamate was achieved in mixed cultures with sulfate-reducing bacteria (Desulfovibrio HL21 or Desulfobulbus propionicus) or methanogens (Methanospirillum hungatei or Methanobrevibacter arboriphilicus AZ). In mixed culture with Desulfovibrio HL21 a μmax of 0.10 h-1 was observed. With Desulfovibrio or the methanogens propionate was a major product (up to 0.47 mol per mol glutamate) in addition to acetate. Extracts of glutamate-grown cells possessed high activities of 3-methylaspartase, a key enzyme of the mesaconate pathway leading to acetate, and very high activities of NAD+-dependent glutamate dehydrogenase, an enzyme most likely involved in the pathway to propionate. The following other substrates allowed reasonable to good growth in pure culture: histidine, α-ketoglutarate, serine, cysteine, glycine, adenine, pyruvate, oxaloacetate and citrate. Utilization in mixed cultures was demonstrated for: glutamine, arginine, ornithine, threonine, lysine, alanine, valine, leucine and isoleucine (with Desulfovibrio HL21) and malate (with Methanospirillum). The shift in the fermentation of glutamate and the syntrophic utilization of the above substrates are explained in terms of interspecies hydrogen transfer. Strain glu 65 is described as the type strain of Acidaminobacter hydrogenoformans gen. nov. sp. nov.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00410730
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  • 3
    Electronic Resource
    Electronic Resource
    Glycerol and dihydroxyacetone dissimilation in Desulfovibrio strains (1987)
    Springer
    Archives of microbiology 147 (1987), S. 249-256 
    Details
    ISSN: 1432-072X
    Keywords: Desulfovibrio ; Glycerol dissimilation ; Glycerol kinase ; Dissimilatory sulfate reduction ; NADH dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract During growth on glycerol two marine Desulfovibrio strains that can grow on an unusually broad range of substrates contained high activities of glycerol kinase, NAD(P)-independent glycerol 3-phosphate dehydrogenase and the other enzymes necessary for the conversion of dihydroxyacetone phosphate to pyruvate. Glycerol dehydrogenase and a specific dihydroxyacetone kinase were absent. During growth on dihydroxyacetone, glycerol kinase is involved in the initial conversion of this compound to dihydroxyacetone phosphate which is then further metabolized. Some kinetic properties of the partially purified glycerol kinase were determined. The role of NAD as electron carrier in the energy metabolism during growth of these strains on glycerol and dihydroxyacetone is discussed. Glycerol also supported growth of three out of four ‘classical’ Desulfovibrio strains tested. D. vulgaris strain Hildenborough grew slowly on glycerol and contained glycerol kinase, glycerol 3-phosphate dehydrogenase and enzymes for the dissimilation of dihydroxyacetone phosphate. In D. gigas which did not grow on glycerol the enzymes glycerol kinase and glycerol 3-phosphate dehydrogenase were absent in lactate-grown cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00463484
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  • 4
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of APS reductase and bisulfite reductase in three Desulfovibrio species (1988)
    Springer
    Archives of microbiology 150 (1988), S. 296-301 
    Details
    ISSN: 1432-072X
    Keywords: Desulfovibrio ; Dissimilatory sulfate reduction ; APS reductase ; Bisulfite reductase ; Enzyme localization ; Immunogold labeling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The localization of APS reductase and bisulfite reductase in Desulfovibrio gigas, D. vulgaris Hildenborough and D. thermophilus was studied by immunoelectron microscopy. Polyclonal antibodies were raised against the purified enzymes from each strain. Cells fixed with formaldehyde/glutaraldehyde were embedded and ultrathin sections were incubated with antibodies and subsequently labeled with protein A-gold. The bisulfite reductase in all three strains and APS reductase in d. gigas and D. vulgaris were found in the cytoplasm. The labeling of d. thermophilus with APS reductase antibodies resulted in a distribution of gold particles over the cytoplasmic membrane region. The localization of the two enzymes is discussed with respect to the mechanism and energetics of dissimilatory sulfate reduction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00407795
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  • 5
    Electronic Resource
    Electronic Resource
    Ethanol dissimilation in Desulfovibrio (1988)
    Springer
    Archives of microbiology 150 (1988), S. 552-557 
    Details
    ISSN: 1432-072X
    Keywords: Desulfovibrio ; Ethanol dissimilation ; Dissimilatory sulfate reduction ; Alcohol dehydrogenase ; Aldehyde dehydrogenase ; NADH dehydrogenase ; Interspecies hydrogen transfer
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract During growth of ethanol plus sulfate Desulfovibrio gigas and three other Desulfovibrio strains tested contained high NAD-dependent alcohol dehydrogenase activities and dye-linked aldehyde dehydrogenase activities. In lactate-grown cells these activities were lower or absent. In D. gigas an NADH dehydrogenase activity was found which was higher during growth on ethanol than during growth on lactate. The NADH dehydrogenase activity appeared to consist of at least three different soluble enzymes. The aldehyde dehydrogenase activity in D. gigas was highest with benzylviologen as an acceptor and was strongly stimulated by potassium ions. Coenzyme A or phosphate dependency could not be shown, indicating that acetyl-CoA or acetyl phosphate are not intermediates in the conversion of acetaldehyde to acetate. In the absence of sulfate D. gigas was able to convert ethanol to acetate by means of interspecies hydrogen transfer to a methanogen. This conversion, however, did not lead to growth of the Desulfovibrio.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408248
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  • 6
    Electronic Resource
    Electronic Resource
    Cleavage of dimethylsulfoniopropionate and reduction of acrylate by Desulfovibrio acrylicus sp. nov. (1996)
    Springer
    Archives of microbiology 166 (1996), S. 109-115 
    Details
    ISSN: 1432-072X
    Keywords: Key words Dimethylsulfoniopropionate ; Dimethylsulfide ; Acrylate ; Anaerobic respiration ; Sulfate-reducing bacterium ; Desulfovibrio acrylicus sp. nov.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract From anoxic intertidal sediment, a dimethylsulfoniopropionate (DMSP)-cleaving anaerobe (strain W218) was isolated that reduced the acrylate formed to propionate. The bacterium was vibrio- to rod-shaped and motile by means of multiple polar flagella. It reduced sulfate, thiosulfate, and acrylate, and used lactate, fumarate, succinate, malate, pyruvate, ethanol, propanol, glycerol, glycine, serine, alanine, cysteine, hydrogen, and formate as electron donors. Sulfate and acrylate were reduced simultaneously; growth with sulfate was faster than with acrylate. Extracts of cells grown in the presence of DMSP contained high DMSP lyase activities (9.8 U/mg protein). The DNA mol% G+C was 45.1. On the basis of its characteristics and the 16S rRNA gene sequence, strain W218 was assigned to a new Desulfovibrio species for which the name Desulfovibrio acrylicus is proposed. A variety of other sulfate-reducing bacteria (eight of them originating from a marine or saline environment and five from other environments) did not reduce acrylate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050363
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  • 7
    Electronic Resource
    Electronic Resource
    Tetrahydrofolate serves as a methyl acceptor in the demethylation of dimethylsulfoniopropionate in cell extracts of sulfate-reducing bacteria (1997)
    Springer
    Archives of microbiology 169 (1997), S. 84-87 
    Details
    ISSN: 1432-072X
    Keywords: Key words Dimethylsulfoniopropionate ; Methylthiopropionate ; Sulfate-reducing bacteria ; Desulfobacterium ; Tetrahydrofolate ; Methyltransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Tetrahydrofolate was shown to function as a methyl acceptor in the anaerobic demethylation of dimethylsulfoniopropionate to methylthiopropionate in cell extracts of the sulfate-reducing bacterium strain WN. Dimethylsulfoniopropionate-dependent activities were 0.56 μmol methyltetrahydrofolate min–1 (mg protein)–1 and were higher than required to explain the growth rate of strain WN on dimethylsulfoniopropionate. The reaction did not require ATP or reductive activation by titanium(III)-nitrilotriacetic acid. Preincubation of the extract under air significantly decreased the activity (35% loss in 3 h). Three other dimethylsulfoniopropionate-demethylating sulfate reducers, Desulfobacterium niacini, Desulfobacterium vacuolatum, and Desulfobacterium strain PM4, had dimethylsulfoniopropionate:tetrahydrofolate methyltransferase activities of 0.16, 0.05, and 0.24 μmol min–1 (mg protein)–1, respectively. No methyltransferase activity to tetrahydrofolate was found with betaine as a substrate, not even in extracts of betaine-grown cells of these sulfate reducers. Dimethylsulfoniopropionate demethylation in cell extracts of strain WN was completely inhibited by 0.5 mM propyl iodide; in the light, the inhibition was far less strong, indicating involvement of a corrinoid-dependent methyltransferase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050545
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  • 8
    Electronic Resource
    Electronic Resource
    Rhodopseudomonas sulfidophila, nov. spec., a new species of the purple nonsulfur bacteria (1973)
    Springer
    Archives of microbiology 92 (1973), S. 45-58 
    Details
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary From marine mud flats a new type of photosynthetic purple bacterium was isolated. This type is described as a new species of the Rhodospirillaceae and is named Rhodopseudomonas sulfidophila. The cells are rod-shaped, 0.6 to 0.9 μ wide and 0.9 to 2.0 μ long, and motile by means of polar flagella. Cell division occurs by binary fission. The photosynthetic membrane system is of the vesicular type. The pigments consist of bacteriochlorophyll a and of carotenoids, most probably of the spheroidene group. A wide range of organic compounds can be utilized anaerobically in the light. Growth on organic compounds aerobically in the dark is also possible. Niacin, thiamin, biotin and p-aminobenzoic acid are required as growth factors. The new species needs 2.5% (w/v) sodium chloride for optimal growth. All strains show excellent photolithotrophic growth on hydrogen, hydrogen sulfide, and thiosulfate. They show a remarkably high sulfide tolerance. Sulfide and thiosulfate are oxidized to sulfate without an intermediate accumulation of elemental sulfur. The new species seems to be one of the most versatile types of photosynthetic bacteria isolated thus far.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409510
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  • 9
    Electronic Resource
    Electronic Resource
    Pathway of propionate formation from ethanol in Pelobacter propionicus (1987)
    Springer
    Archives of microbiology 147 (1987), S. 321-327 
    Details
    ISSN: 1432-072X
    Keywords: Propionate formation ; Ethanol fermentation ; Succinate pathway ; Petobacter propionicus ; Cytochrome b ; Anaerobic electron transport ; Pyruvate synthase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Whole cells of Pelobacter propionicus fermented (1-13C) ethanol and CO2 to nearly equal amounts of (2-13C) and (3-13C) propionate and to (1-13C) acetate indicating a randomizing pathway of propionate formation. Enzymes involved in the fermentation were assayed in cell-free extracts and cetyltrimethylammonium bromide-permeabilized cells grown with ethanol as sole substrate. Alcohol dehydrogenase, aldehyde dehydrogenase (benzylviologen-reducing), phosphate acetyl transferase, acetate kinase, pyruvate synthase, methylmalonyl CoA: pyruvate transcarboxylase, propionyl CoA: succinate CoA transferase, and the enzymes of the succinate-methylmalonyl CoA pathway all were detected at activities sufficient to be involved in ethanol fermentation. Very low amounts of a b-type cytochrome were detected in ethanol-grown cells (46 nmol δ g protein−1). Low cell yields obtained with ethanol as substrate indicate that P. propionicus does not conserve energy by electron transport-linked fumarate reduction. Despite the presence of a hydrogenase and a shift in the fermentation of lactate towards the formation of more propionate in the presence of hydrogen, P. propionicus was unable, to catalyze, the reduction of acetate and CO2 to propionate, unlike Desulfobulbus propionicus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00406127
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  • 10
    Electronic Resource
    Electronic Resource
    Purification and characterization of an alcohol dehydrogenase from 1,2-propanediol-grown Desulfovibrio strain HDv (1995)
    Springer
    Archives of microbiology 164 (1995), S. 265-270 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsDesulfovibrio strain HDv ; Dissimilatory sulfate reduction ; Alcohol dehydrogenase ; 1 ; 2-Propanediol dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The sulfate-reducing bacterium Desulfovibrio strain HDv (DSM 6830) grew faster on (S)- and on (R, S)-1,2-propanediol (μmax 0.053 h–1) than on (R)-propanediol (0.017 h–1) and ethanol (0.027 h–1). From (R, S)-1,2-propanediol-grown cells, an alcohol dehydrogenase was purified. The enzyme was oxygen-labile, NAD-dependent, and decameric; the subunit mol. mass was 48 kDa. The N-terminal amino acid sequence indicated similarity to alcohol dehydrogenases belonging to family III of NAD-dependent alcohol dehydrogenases, the first 21 N-terminal amino acids being identical to those of the Desulfovibrio gigas alcohol dehydrogenase. Best substrates were ethanol and propanol (K m of 0.48 and 0.33 mM, respectively). (R, S)-1,2-Propanediol was a relatively poor substrate for the enzyme, but activities in cell extracts were high enough to account for the growth rate. The enzyme showed a preference for (S)-1,2-propanediol over (R)-1,2-propanediol. Antibodies raised against the alcohol dehydrogenase of D. gigas showed cross-reactivity with the alcohol dehydrogenase of Desulfovibrio strain HDv and with cell extracts of six other ethanol-grown sulfate-reducing bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050263
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