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  • 1
    Electronic Resource
    Electronic Resource
    The dissimilatory sulfite reductase from Desulfosarcina variabilis is a desulforubidin containing uncoupled metalated sirohemes and S = 9/2 iron-sulfur clusters (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 10323-10330 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00090a007
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  • 2
    Electronic Resource
    Electronic Resource
    Pathway of propionate formation in Desulfobulbus propionicus (1984)
    Springer
    Archives of microbiology 139 (1984), S. 167-173 
    Details
    ISSN: 1432-072X
    Keywords: Propionate formation ; 13C NMR ; Desulfobulbus propionicus ; Sulfate reducing bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Whole cells of Desulfobulbus propionicus fermented [1-13C]ethanol to [2-13C] and [3-13C]propionate and [1-13C]-acetate, which indicates the involvement of a randomizing pathway in the formation of propionate. Cell-free extracts prepared from cells grown on lactate (without sulfate) contained high activities of methylmalonyl-CoA: pyruvate transacetylase, acetase kinase and reasonably high activities of NAD(P)-independent L(+)-lactate dehydrogenase NAD(P)-independent pyruvate dehydrogenase, phosphotransacetylase, acetate kinase and reasonably high activity of NAD(P)-independent L(+)-lactate dehydrogenase, fumarate reductase and succinate dehydrogenase. Cell-free extracts catalyzed the conversion of succinate to propionate in the presence of pyruvate, CoA and ATP and the oxaloacetate-dependent conversion of propionate to succinate. After growth on lactate or propionate in the presence of sulfate similar enzyme levels were found except for fumarate reductase which was considerably lower. Fermentative growth on lactate led to higher cytochrome b contents than growth with sulfate as electron acceptor. The labeling studies and the enzyme measurements demonstrate that in Desulfobulbus propionate is formed via a succinate pathway involving a transcarboxylase like in Propionibacterium. The same pathway may be used for the degradation of propionate to acetate in the presence of sulfate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00401994
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  • 3
    Electronic Resource
    Electronic Resource
    Selenomonas acidaminovorans sp. nov., a versatile thermophilic proton-reducing anaerobe able to grow by decarboxylation of succinate to propionate (1992)
    Springer
    Archives of microbiology 157 (1992), S. 169-175 
    Details
    ISSN: 1432-072X
    Keywords: Fermentation of amino acids ; Interspecies hydrogen transfer ; Propionic acid fermentation ; Selenomonas acidaminovorans ; Succinate decarboxylation ; Syntrophic degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A moderately thermophilic anaerobic bacterium (strain Su883), which decarboxylated succinate to propionate, was isolated from granular methanogenic sludge. The bacterium appeared to ferment a number of amino acids including glutamate, histidine, arginine, ornithine, citrulline, and threonine to propionate, acetate and hydrogen. Propionate was formed via the oxidative decarboxylation of α-ketoglutarate to succinyl-CoA. In addition, the strain degraded glucose, fructose, glycerol, pyruvate, serine, alanine, citrate and malate to acetate, carbon dioxide and hydrogen, and branched-chain amino acids to branched-chain fatty acids. With all single substrates solely hydrogen was formed as reduced fermentation product. Mixed cultures of strain Su883 and Methanobacterium thermoautotrophicum ΔH showed a more rapid conversion of substrates and with some substrates a shift from acetate to propionate formation. Strain Su883 is a motile, gram-negative, non-sporeforming, slightly curved rod with a DNA base ratio of 56.5 mol% guanine-plus-cytosine. Selenomonas acidaminovorans Su883 is proposed as type strain for the new species within the genus Selenomonas.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245286
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  • 4
    Electronic Resource
    Electronic Resource
    Investigation of the fumarate metabolism of the syntrophic propionate-oxidizing bacterium strain MPOB (1998)
    Springer
    Archives of microbiology 169 (1998), S. 346-352 
    Details
    ISSN: 1432-072X
    Keywords: Key words Syntrophy ; Fumarate reduction ; Propionate ; oxidation ; Anaerobic growth ; Electron transport chain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The growth of the syntrophic propionate-oxidizing bacterium strain MPOB in pure culture by fumarate disproportionation into carbon dioxide and succinate and by fumarate reduction with propionate, formate or hydrogen as electron donor was studied. The highest growth yield, 12.2 g dry cells/mol fumarate, was observed for growth by fumarate disproportionation. In the presence of hydrogen, formate or propionate, the growth yield was more than twice as low: 4.8, 4.6, and 5.2 g dry cells/mol fumarate, respectively. The location of enzymes that are involved in the electron transport chain during fumarate reduction in strain MPOB was analyzed. Fumarate reductase, succinate dehydrogenase, and ATPase were membrane-bound, while formate dehydrogenase and hydrogenase were loosely attached to the periplasmic side of the membrane. The cells contained cytochrome c, cytochrome b, menaquinone-6 and menaquinone-7 as possible electron carriers. Fumarate reduction with hydrogen in membranes of strain MPOB was inhibited by 2-(heptyl)-4-hydroxyquinoline-N-oxide (HOQNO). This inhibition, together with the activity of fumarate reductase with reduced 2,3-dimethyl-1,4-naphtoquinone (DMNH2) and the observation that cytochrome b of strain MPOB was oxidized by fumarate, suggested that menequinone and cytochrome b are involved in the electron transport during fumarate reduction in strain MPOB. The growth yields of fumarate reduction with hydrogen or formate as electron donor were similar to the growth yield of Wolinella succinogenes. Therefore, it can be assumed that strain MPOB gains the same amount of ATP from fumarate reduction as W. succinogenes, i.e. 0.7 mol ATP/mol fumarate. This value supports the hypothesis that syntrophic propionate-oxidizing bacteria have to invest two-thirds of an ATP via reversed electron transport in the succinate oxidation step during the oxidation of propionate. The same electron transport chain that is involved in fumarate reduction may operate in the reversed direction to drive the energetically unfavourable oxidation of succinate during syntrophic propionate oxidation since (1) cytochrome b was reduced by succinate and (2) succinate oxidation was similarly inhibited by HOQNO as fumarate reduction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050581
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  • 5
    Electronic Resource
    Electronic Resource
    Metabolism of l-alanine in Desulfotomaculum ruminis and two marine Desulfovibrio strains (1986)
    Springer
    Archives of microbiology 145 (1986), S. 277-279 
    Details
    ISSN: 1432-072X
    Keywords: Sulfate reduction ; Desulfotomaculum ruminis ; Desulfovibrio ; Alanine degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The degradation of l-alanine by three strains of sulfate-reducing bacteria that can grow with l-alanine as an energy source was investigated. In Desulfotomaculum ruminis and most likely also in two marine Desulfovibrio strains alanine is converted to pyruvate via an NAD-dependent alanine dehydrogenase. D. ruminis contained high activities of soluble NADH and NADPH dehydrogenases. In the marine strains the activities were much lower and the NADH dehydrogenase was partly associated with the membrane fraction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00443658
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  • 6
    Electronic Resource
    Electronic Resource
    A fluoride-insensitive inorganic pyrophosphatase isolated from Methanothrix soehngenii (1992)
    Springer
    Archives of microbiology 157 (1992), S. 284-289 
    Details
    ISSN: 1432-072X
    Keywords: Methanothrix soehngenii ; Acetate degradation ; Energetics ; Inorganic pyrophosphatase ; Fluoride inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An inorganic pyrophosphatase [E.C. 3.6.1.1] was isolated from Methanothrix soehngenii. In three steps the enzyme was purified 400-fold to apparent homogeneity. The molecular mass estimated by gelfiltration was 139±7 kDa. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis indicated that the enzyme is composed of subunits with molecular masses of 35 and 33 kDa in an α 2 β 2 oligomeric structure. The enzyme catalyzed the hydrolysis of inorganic pyrophosphate, tri-and tetrapolyphosphate, but no activity was observed with a variety of other phosphate esters. The cation Mg2+ was required for activity. The pH optimum was 8 at 1 mM PP i and 5 mM Mg2+. The enzyme was heat-stable, insensitive to molecular oxygen and not inhibited by fluoride. Analysis of the kinetic properties revealed an apparent K m for PP i of 0.1 mM in the presence of 5 mM Mg2+. The V max was 590 μmol of pyrophosphate hydrolyzed per min per mg protein, which corresponds to a K cat of 1400 per second. The enzyme was found in the soluble enzyme fraction after ultracentrifugation, when cells were disrupted by French Press. Upto 5% of the pyrophosphatase was associated with the membrane fraction, when gentle lysis procedyre were applied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245163
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  • 7
    Electronic Resource
    Electronic Resource
    Pathway of propionate formation in Desulfobulbus propionicus (1985)
    Springer
    Archives of microbiology 140 (1985), S. 298-298 
    Details
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446965
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  • 8
    Electronic Resource
    Electronic Resource
    d-Xylose catabolism in Bacteroides xylanolyticus X5-1 (1994)
    Springer
    Archives of microbiology 161 (1994), S. 521-527 
    Details
    ISSN: 1432-072X
    Keywords: Pentose phosphate pathway ; Embden-Meyerhof-Parnas pathway ; Phosphoketolase pathway ; Bacteroides xylanolyticus X5-1 ; Xylose catabolism ; Energy conservation ; Cofactor regeneration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The xylose metabolism of Bacteroides xylanolyticus X5-1 was studied by determining specific enzyme activities in cell free extracts, by following 13C-label distribution patterns in growing cultures and by mass balance calculations. Enzyme activities of the pentose phosphate pathway and the Embden-Meyerhof-Parnas pathway were sufficiently high to account for in vivo xylose fermentation to pyruvate via a combination of these two pathways. Pyruvate was mainly oxidized to acetyl-CoA, CO2 and a reduced cofactor (ferredoxin). Part of the pyruvate was converted to acetyl-CoA and formate by means of a pyruvate-formate lyase. Acetyl-CoA was either converted to acetate by a combined action of phosphotransacetylase and acetate kinase or reduced to ethanol by an acetaldehyde dehydrogenase and an ethanol dehydrogenase. The latter two enzymes displayed both a NADH- and a NADPH-linked activity. Cofactor regeneration proceeded via a reduction of intermediates of the metabolism (i.e. acetyl-CoA and acetaldehyde) and via proton reduction. According to the deduced pathway about 2.5 mol ATP are generated per mol of xylose degraded.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307774
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  • 9
    Electronic Resource
    Electronic Resource
    Phylogenetic analysis of Syntrophobacter wolinii reveals a relationship with sulfate-reducing bacteria (1993)
    Springer
    Archives of microbiology 160 (1993), S. 238-240 
    Details
    ISSN: 1432-072X
    Keywords: Syntrophobacter wolinii ; Syntrophic bacteria ; Sulfate ; reducing bacteria ; PCR ; 16S rRNA ; Phylogeny
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A 16S rRNA sequence analysis of Syntrophobacter wolinii was done by using PCR amplification of the 16S rRNA-genes from DNA isolated from the S. wolinii-Desulfovibrio sp. coculture. Phylogenetic analysis using the obtained sequence revealed that S. wolinii was not related to bacteria growing syntrophically on other fatty acids than propionate, but was related to sulfate-reducing bacteria. The closest related bacteria are Desulfomonile tiedjei and Desulfoarculus baarsii.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00249130
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  • 10
    Electronic Resource
    Electronic Resource
    Formation of l-alanine as a reduced end product in carbohydrate fermentation by the hyperthermophilic archaeon Pyrococcus furiosus (1994)
    Springer
    Archives of microbiology 161 (1994), S. 168-175 
    Details
    ISSN: 1432-072X
    Keywords: Pyrococcus furiosus ; Hyperthermophile ; Archaea ; Fermentation ; l-alanine ; Alanine aminotransferase ; Glutamate dehydrogenase ; Interspecies hydrogen transfer
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The hyperthermophilic archaeon Pyrococcus furiosus was found to form substantial amounts of l-alanine during batch growth on either cellobiose, maltose or pyruvate. Acetate, CO2 and H2 were produced next to alanine. The carbon- and electron balances were complete for all three substrates. Under standard growth conditions (N2/CO2 atmosphere) an alanine/acetate ratio of about 0.3 was found for either substrate. The alanine /acetate ratio was influenced, however, by the hydrogen partial pressure. In the presence of S0 or in coculture with Methanococcus jannaschii this ratio was only 0.07, whereas under a H2/CO2 atmosphere this ratio could amount up to 0.8. Alanine formation was also aflected by the NH inf4 sup+ concentration, i.e. below 4 mM, NH inf4 sup+ becomes limiting to alanine formation. Alanine formation was shown to occur via an alanine aminotransferase, which exhibited a specific activity in cell-free extract of up to 6.0 U/mg (90°C; direction of pyruvate formation). The alanine aminotransferase probably cooperates with glutamate dehydrogenase (up to 23 U/mg; 90°C) and ferredoxin: NADP+ oxidoreductase (up to 0.7 U/mg, using methyl viologen; 90°C) to recycle the electron acceptors involved in catabolism. Thus, the existence of this unusual alanine-forming branch enables P. furiosus to adjust its fermentation, depending on the redox potential of the terminal electron acceptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00276479
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