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  • 1
    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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  • 2
    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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  • 3
    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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  • 4
    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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  • 5
    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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  • 6
    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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  • 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
    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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  • 10
    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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