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  • 11
    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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  • 12
    Electronic Resource
    Electronic Resource
    Anaerobic degradation of betaine by marine Desulfobacterium strains (1989)
    Springer
    Archives of microbiology 152 (1989), S. 393-396 
    Details
    ISSN: 1432-072X
    Keywords: Betaine ; Desulfobacterium strains ; N,N-dimethylglycine ; Sulfate-reducing bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract From enrichment cultures with betaine (20 mM) and sulfate (20 mM) as the substrates and intertidal mud as an inoculum, a betaine-oxidizing, sulfate-reducing bacterium (strain PM4) was isolated. Strain PM4 was an oval to rod-shaped, Gram-negative, motile bacterium, which was able to oxidize lactate completely to CO2 and contained, during growth on betaine and sulfate, high activities of key enzymes of the acetyl CoA/CO dehydrogenase pathway (carbon monoxide dehydrogenase and formate dehydrogenase), but not of 2-oxo-glutarate dehydrogenase, a key enzyme of the citric acid cycle. On the basis of its morphological and physiological characteristics, strain PM4 was identified as a Desulfobacterium strain. Desulfobacterium PM4 grew on betaine with a doubling time of approximately 20 h at 30°C and produced N, N-dimethylglycine (in a 1:1 ratio) and sulfide as products. In this type of betaine metabolism one of the methyl groups of betaine is oxidized to CO2 and the reducing equivalents generated are used for the reduction of sulfate. Desulfobacterium autotrophicum (DSM 3382) grew also on betaine and sulfate with the formation of N,N-dimethylglycine, sulfide and CO2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425179
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  • 13
    Electronic Resource
    Electronic Resource
    Effects of tungstate on the growth of Desulfovibrio gigas NCIMB 9332 and other sulfate-reducing bacteria with ethanol as a substrate (1994)
    Springer
    Archives of microbiology 162 (1994), S. 143-147 
    Details
    ISSN: 1432-072X
    Keywords: Key words     Desulfovibrio gigas ; Dissimilatory sulfate reduction ; Tungstate-stimulated growth ; Aldehyde ; dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract      Growth of Desulfovibrio gigas NCIMB 9332 in mineral, vitamin-supplemented media with ethanol as substrate was strongly stimulated by the addition of tungstate (optimal level approximately 10–7 M). At suboptimal tungstate concentrations, up to 1.0 mM acetaldehyde was detected in the culture supernatant and growth was slow. Omission of both tungstate and molybdate from the media prevented growth and ethanol utilization. Tungstate-deprived cultures that were grown on lactate had much lower aldehyde dehydrogenase (benzylviologen as acceptor; BV-AlDH) levels than tungstate-supplemented cultures. These data suggest that tungstate is required for the synthesis of active BV-AlDH. The characteristics of the enzyme activities in cell-free extracts show that the BV-AlDH activity present in tungstate-supplemented cultures is not due to the recently characterized molybdenum-containing aldehyde dehydrogenase of D. gigas. Out of 13 other strains of ethanol-oxidizing, gram-negative, sulfate-reducing bacteria tested, most strains grew well with either tungstate or molybdate supplementation. In contrast to a recent report, good growth on ethanol of two D. baculatus (Desulfomicrobium) strains (DSM 1741 and DSM 1743) was observed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050116
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  • 14
    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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  • 15
    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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  • 16
    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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  • 17
    Electronic Resource
    Electronic Resource
    Catabolism of malate and related dicarboxylic acids in various Desulfovibrio strains and the involvement of an oxygen-labile NADPH dehydrogenase (1988)
    Springer
    Archives of microbiology 151 (1988), S. 34-39 
    Details
    ISSN: 1432-072X
    Keywords: Desulfovibrio ; Dicarboxylic acids ; l-Malate ; NADPH dehydrogenase ; Dissimilatory sulfate reduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Four out of five Desulfovibrio strains tested were able to oxidize l-malate to acetate in the presence of sulfate. Fumarate and succinate were also oxidized to acetate by these strains, but growth with the latter substrate was marginal. During growth on malate high NADP-dependent malic enzyme and NADPH DH activities were found in all strains. These activities were lower in lactate-or pyruvate-grown cells. An NADPH DH from D. gigas was partially purified. It was oxygen-labile, very sensitive to heavy metal ions and highly specific for NADPH. Growth yield studies indicated that energy conservation occurred during the transport of reducing equivalents from NADPH to the sulfate reduction pathway.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00444665
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  • 18
    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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  • 19
    Electronic Resource
    Electronic Resource
    A rod-shaped, gram-negative, propionigenic bacterium with a wide substrate range and the ability to fix molecular nitrogen (1990)
    Springer
    Archives of microbiology 155 (1990), S. 42-45 
    Details
    ISSN: 1432-072X
    Keywords: Propionic fermentation ; Fermentation of aspartate ; Nitrogen fixation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract From estuarine mud a rod-shaped, motile, gram-negative, anaerobic bacterium was isolated (strain asp 66). Asp 66 fermented several substrates including glucose, fructose, malate, fumarate, citrate and aspartate. Fermentation products were acetate, propionate and presumably CO2. Hydrogen was never formed nor utilized. Succinate conversion to propionate was catalyzed by cell suspensions but did not support growth. Asp 66 did not require vitamins and grew well in mineral media with a fermentable substrate. The pH range for growth was from 6.5 to 8.5. Temperature optimum was 27 to 30°C. The strain was able to fix N2 as evidenced by its growth with N2 as sole nitrogen source and its ability to reduce acetylene to ethylene. Cell-free extracts of cultures grown under air without shaking contained cytochrome(s) with absorption peaks at 523 nm and at 553 nm. The G+C content of the DNA was 60.8+-1 mol%. The taxonomic position of strain asp 66 is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00291272
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  • 20
    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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