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  • 1
    Electronic Resource
    Electronic Resource
    Function of fumarate reductase in methanogenic bacteria (Methanobacterium) (1978)
    Springer
    Archives of microbiology 119 (1978), S. 215-218 
    Details
    ISSN: 1432-072X
    Keywords: Methanobacterium thermoautotrophicum ; ATP synthesis ; Funtarate reductase ; Menaquinone ; Cytochromeb ; Succinate dehydrogenase ; α-Ketoglutarate synthesis ; Succinate incorporation ; Fumarate incorporation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Methanogenic bacteria contain high activities of fumarate reductase. An interesting hypothesis has recently been advanced that this enzyme, in cooperation with a succinate dehydrogenase, functions in a fumarate-succinate cycle for ATP synthesis. This hypothesis was tested by determining whether [2, 3-3H] succinate loses3H when taken up by growing cells.Methanobacterium thermoautotrophicum was grown on H2 plus CO2 in the presence of [U-14C, 2,3-3H] succinate. The double labelled dicarboxylic acid was found to be incorporated into cell material with the loss of only 30% of tritium. Neither was3H released into H2O in significant amounts. This finding excludes a catabolic oxidation of succinate to fumarate in the growing cells and thus the operation of a fumaratesuccinate cycle. It is shown that the function of fumarate reductase inM. thermoautotrophicum is to provide the cells with succinate for the synthesis of α-ketoglutarate, an intermediate in glutamate, arginine and proline synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00964276
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  • 2
    Electronic Resource
    Electronic Resource
    ATP-driven succinate oxidation in the catabolism of Desulfuromonas acetoxidans (1986)
    Springer
    Archives of microbiology 144 (1986), S. 78-83 
    Details
    ISSN: 1432-072X
    Keywords: Desulfuromonas acetoxidans ; Succinate oxidation ; Sulphur reduction ; Acetate oxidation ; Citric acid cycle ; Reverse of electron transport ; Menaquinone ; ATP synthase ; Succinate dehydrogenase ; Sulphur reductase ; NADH dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The oxidation of succinate with elemental sulphur in Desulfuromonas acetoxidans was investigated using a membrane preparation of this bacterium. The following results were obtained: 1. The preparation catalyzed the oxidation of succinate with sulphur and NAD. These reactions were dependent on ATP and were abolished by the presence of protonophores or dicyclohexylcarbodiimide (DCCD). 2. The membrane preparation also catalyzed the reduction of fumarate with H2S or with NADH. These activities were not dependent on ATP and were not affected by protonophores or DCCD. 3. By extraction-reincorporation experiments it could be shown that menaquinone is involved in electron transport between H2S and fumarate and between NADH and fumarate. 4. The membrane fraction catalyzed the reduction of the water-soluble menaquinone-analogue dimethylnaphthoquinone (DMN) by succinate, H2S, or NADH, and the oxidation of DMNH2 by fumarate. These activities were not dependent on the presence of menaquinone and were not influenced by ATP. 5. The activities involving succinate oxidation or fumarate reduction were similarly sensitive to 2(n-nonyl)-4-hydroxyquinoline-N-oxide, while H2S and NADH oxidation by DMN were not affected by the inhibitor. It is concluded that the catabolism of D. acetoxidans involves the energy-driven oxidation of succinate with elemental sulphur or NAD as electron acceptors and that menaquinone is a component of the electron transport chain catalyzing these reactions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00454960
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  • 3
    Electronic Resource
    Electronic Resource
    Membrane-bound NADPH dehydrogenase- and ferredoxin: NADP oxidoreductase activity involved in electron transport during acetate oxidation to CO2 in Desulfobacter postgatei (1988)
    Springer
    Archives of microbiology 150 (1988), S. 145-154 
    Details
    ISSN: 1432-072X
    Keywords: Acetate oxidation ; Citric acid cycle ; ATPase ; Energy conservation ; Electron transport ; Ferredoxin: NADP oxidoreductase ; NADPH dehydrogenase ; Succinate dehydrogenase ; Malate dehydrogenase ; Heptylhydroxyquinoline-N-oxide ; Sulfate-reducing bacteria ; Desulfobacter postgatei
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Desulfobacter postgatei grows on acetate and sulfate as energy source. The oxidation of acetate to 2 CO2 proceeds via the citric acid cycle involving membrane-bound succinate dehydrogenase and membrane-bound malate dehydrogenase. We report here that the organism contains membrane-bound NADPH dehydrogenase and ferredoxin: NADP oxidoreductase for the reoxidation of NADPH and reduced ferredoxin generated during isocitrate- and 2-oxoglutarate oxidation, respectively. The presence of proton translocating ATPase activity is also described. NADPH dehydrogenase and succinate dehydrogenase were found to be electrically connected within the membrane and electron transfer between these two enzymes was shown to be coupled with proton translocation. The membrane fraction catalyzed the oxidation of NADPH with fumarate and the reduction of NADP with succinate. NADPH oxidation with fumarate was stimulated by protonophores and inhibited by the proton translocating ATPase inhibitor dicyclohexylcarbodiimide (DCCD) and by heptylhydroxyquinoline-N-oxide (HQNO); inhibition by DCCD was relieved by protonophores. NADP reduction with succinate was dependent on ATP and inhibited by protonophores, DCCD, and HQNO. The membrane fraction also mediated the oxidation of NADPH with the water soluble menaquinone analogue dimethylnaphthoquinone (DMN) and the reduction of fumarate with DMNH2. Only the former reaction was stimulated by protonophores and only the latter reaction was inhibited by HQNO. This suggests that the NADPH dehydrogenase reaction is the site of energy conservation and the succinate dehydrogenase is the site of HQNO inhibition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425154
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  • 4
    Electronic Resource
    Electronic Resource
    Anaerobic acetate oxidation to CO2 by Desulfobacter postgatei (1983)
    Springer
    Archives of microbiology 136 (1983), S. 222-229 
    Details
    ISSN: 1432-072X
    Keywords: Desulfobacter postgatei ; Citric acid cycle ; Anaplerotic reactions ; Citrate (si)-synthase ; 2-Oxoglutarate:ferredoxin oxidoreductase ; Succinate dehydrogenase ; Succinyl-CoA:acetate CoA transferase ; Acetyl-CoA synthetase ; Pyruvate synthase ; Phosphoenolpyruvate synthetase ; Phosphoenolpyruvate carboxylase ; Menaquinone ; Ferredoxin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The strict anaerobe Desulfobacter postgatei oxidizes acetate to CO2 with sulfate as electron acceptor. During growth at 28°C with a doubling time of 16 h the oxidation and assimilation rate of acetate were 280 nmol and 20 nmol per min and mg protein, respectively. In cell extracts all the enzymes of the citric acid cycle were found (numbers in brackets=specific activities in nmol per min and mg protein at 28°C): Citrate (si)-synthase (250); aconitase (200); NADP-dependent isocitrate dehydrogenase (8500); 2-oxoglutarate: ferredoxin oxidoreductase (300); succinyl-CoA: acetate CoA transferase (160); membrane bound succinate dehydrogenase (3500); and membrane bound malate dehydrogenase with 2,3-dimethyl-1,4-naphthoquinone as artificial electron acceptor (54). The following enzymes catalyzing the synthesis of oxaloacetate from acetate and CO2 were also present: Acetyl-CoA synthetase (10); ferredoxin dependent pyruvate synthase (30); phosphoenolpyruvate synthetase (10); and phosphoenolpyruvate carboxylase (24). The key enzymes of the glyoxylate cycle were not detected. The order of magnitude of the observed enzyme activities was sufficient to account for an oxidation of acetate via the citric acid cycle and for a synthesis of oxaloacetate from acetate and CO2 as anaplerotic reaction. The membranes of D. postgatei contained menaquinone (0.35 nmol per mg cell dry weight) rather than ubiquinone or demethylmenaquinone. The cytoplasmic fraction contained ferredoxin (0.09 nmol per mg cell dry weight).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409849
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  • 5
    Electronic Resource
    Electronic Resource
    Mechanism of acetate oxidation to CO2 with elemental sulfur in Desulfuromonas acetoxidans (1985)
    Springer
    Archives of microbiology 141 (1985), S. 392-398 
    Details
    ISSN: 1432-072X
    Keywords: Desulfuromonas acetoxidans ; Acetate oxidation ; Sulfur reduction ; Acetate activation ; Citric acid cycle ; Anaplerotic reaction ; Citrate (si)-synthase ; Succinate dehydrogenase ; Succinyl-CoA: acetate CoA transferase ; 2-Oxoglutarate: ferredoxin oxidoreductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The strict anaerobe Desulfuromonas acetoxidans can oxidize acetate to CO2 with elemental sulfur as electron acceptor. 14C-labelling experiments and enzyme studies are described revealing that acetate oxidation proceeds via the citric acid cycle with the synthesis of oxaloacetate from acetate and 2 CO2 via pyruvate as anaplerotic reaction. An oxidation of acetate via one carbon unit intermediates as proposed for anaerobic bacteria fermenting acetate to 2 CO2 and 4 H2 was excluded.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00428855
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