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