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  • 1
    ISSN: 1432-072X
    Keywords: Growth yield ; Vibrio succinogenes ; ATP ; Fumarate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Vibrio succinogenes which gains all the ATP by anaerobic electron transport phosphorylation, was grown in continuous culture on a defined medium with formate and fumarate as sole energy sources. The growth yield at infinite dilution rate (Y max) was obtained by extrapolation from the growth yields measured at various dilution rates. With formate as the growth limiting substrate, Y max was found as 14 g dry cells/mol formate. Under these conditions growth was limited by the rate of energy supply, because formate is used only as a catabolic substrate (Bronder et al. 1982). The Y ATP max calculated from the ATP requirement for cell synthesis was 18 g dry cells/mol ATP. This gives an ATP/2e ratio of 0.8. The ATP/2e ratio in vitro had been measured as 1 (Kröger and Winkler 1981). It is concluded that growing V. succinogenes gain at least 80% the stoichiometrically possible amount of ATP, when growth is limited by energy supply.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-072X
    Keywords: Fumarate ; Vibrio succinogenes ; Biosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. With fumarate as the terminal electron acceptor and either H2 or formate as donor, Vibrio succinogenes could grow anaerobically in a mineral medium using fumarate as the sole carbon source. Both the growth rate and the cell yield were increased when glutamate was also present in the medium. 2. Glutamate was incorporated only into the amino acids of the glutamate family (glutamate, glutamine, proline and arginine) of the protein. The residual cell constituents were synthesized from fumarate. 3. Pyruvate and phosphoenolpyruvate, as the central intermediates of most of the cell constituents, were formed through the action of malic enzyme and phosphoenolpyruvate synthetase. Fructose-1,6-bisphosphate aldolase was present in the bacterium suggesting that this enzyme is involved in carbohydrate synthesis. 4. In the absence of added glutamate the amino acids of the glutamate family were synthesized from fumarate via citrate. The enzymes involved in glutamate synthesis were present. 5. During growth in the presence of glutamate, net reducing equivalents were needed for cell synthesis. Glutamate and not H2 or formate was used as the source of these reducing equivalents. For this purpose part of the glutamate was oxidized to yield succinate and CO2. 6. The α-ketoglutarate dehydrogenase involved in this reaction was found to use ferredoxin as the electron acceptor. The ferredoxin of the bacterium was reoxidized by means of a NADP-ferredoxin oxidoreductase. Enzymes catalyzing the reduction of NAD, NADP or ferredoxin by H2 or formate were not detected in the bacterium.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 144 (1986), S. 78-83 
    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
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  • 4
    ISSN: 1432-072X
    Keywords: Wolinella succinogenes ; Sulfur cycle ; H2S oxidation ; Sulfur reduction ; Fumarate reduction ; Formate oxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Wolinella succinogenes was found to grow on H2S plus fumarate with the formation of elemental sulfur and succinate. The growth rate was 0.18 h-1 (t d=3.8 h) and the growth yield was estimated to be 6.0 g per mol fumarate used. Growth also occurred on formate plus elemental sulfur; the products formed were H2S and CO2. The growth rate and estimated growth yield were 0.58 h-1 (t d=1.2 h) and 3.5 g per mol formate used, respectively. These results suggest that certain chemotrophic anaerobes may be involved in both the formation and reduction of sulfur.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 155 (1990), S. 62-67 
    ISSN: 1432-072X
    Keywords: Menaquinone ; Succinate respiration ; Electron transport ; Bacillus subtilis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The question was investigated as to whether the bacterial menaquinone (MK) is a component of the electron transport chain catalyzing succinate respiration in Bacillus subtilis. Three different methods were applied, and the following consistent results were obtained. (i) Solvent extraction of MK from the bacterial membrane caused total inhibition of the respiratory activities with succinate and NADH, while the activity of succinate dehydrogenase remained unaffected. The respiratory activities were restored onincorporation of vitamin K1 into the membrane preparation. (ii) The membrane fraction of a B. subtilis mutant containing 15% of the wild-type amount of MK, respired succinate and NADH at reduced activities. Wild-type activities were restored on fusion of the preparation to liposomes containing vitamin K1. (iii) The membrane fraction of B. subtilis catalyzed succinate oxidation by various water-soluble naphtho- or benzoquinones at specific activities exceeding to that of succinate respiration. The results suggest that MK is involved in succinate respiration, although its redox potential is unfavorable.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-072X
    Keywords: Key words Sulfur reduction ; Polysulfide ; Wolinella ; succinogenes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Wolinella succinogenes grows by anaerobic respiration with formate and polysulfide. Polysulfide forms spontaneously from sulfur and sulfide. Here we report that this eubacterium also grows with formate and elemental sulfur under conditions that do not allow polysulfide formation. With the appropriate amount of Fe2+ added to the medium, the concentration of polysulfide was calculated to be 0.4 nM, which is 1/400th of the concentration that of dissolved elemental sulfur. At commensurable growth rates, the growth yield with sulfur was one quarter of that with polysulfide as electron acceptor. The same low growth yield either with sulfur or with polysulfide as electron acceptor was measured for a Δpsr mutant that lacks the genes encoding polysulfide reductase (Psr).
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 129 (1981), S. 100-104 
    ISSN: 1432-072X
    Keywords: P/fumarate ratio ; Fumarate reduction ; Phosphorylation ; Vibrio succinogenes ; Uncouplers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. Cells of Vibrio succinogenes, treated with EDTA at pH 8, catalyze the phosphorylation of their endogenous ADP and AMP as a function of the electron transport from formate to fumarate. The P/fumarate ratio obtained from the initial velocity of the phosphorylation on initiation of the electron transport and from the activity of fumarate reduction in the steady state was 0.90. The phosphorylation was prevented by 10μmol/g protein carbonylcyanide-3-chlorophenylhydrazone. 2. The esterification of external phosphate in the presence of ADP, hexokinase and glucose is catalysed by a membrane preparation of V. succinogenes in the steady state of fumarate reduction by H2. The phosphorylation was fully abolished by either 5μmol/g protein carbonylcyanide-4-trifluoromethoxyphenylhydrazone or 30μmol/g protein carbonylcyanide-3-chlorphenylhydrazone. Phosphorylation was blocked also by dicyclohexylcarbodiimide, an inhibitor of the Mg2+-dependent membrane bound ATP synthase, and by low concentrations of the inhibitors of electron transport 2-(n-nonyl)-4-hydroxyquinoline-N-oxide or 4-chloromercuriphenylsulfonate. 3. The P/fumarate ratios, measured with the membrane preparation, were found to increase with progressive inhibition of the electron transport from hydrogen to fumarate by means of 4-chloromercuriphenylsulfonate. The extrapolated ratio at vanishing electron transport activity was 0.47. 4. About 50% of the membrane preparation was found to consist of inverted vesicles with the hydrogenase and formate dehydrogenase oriented to the inside. The residual part is considered as being incapable of performing energy transduction. The extrapolated P/fumarate ratio valid for the inverted vesicles was 0.94.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-072X
    Keywords: Phosphorylative nitrite reduction ; Nitrate reduction ; Vibrio succinogenes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. Growth of Vibrio succinogenes with nitrate as terminal electron acceptor was found to be a function of the following two catabolic reactions: (a) $$HCO _2^ - + NO _3^ - + H^ + \to CO_2 + NO _2^ - + H_2 O$$ (b) $$3HCO _2^ - + NO _2^ - + 5H^ + \to 3CO_2 + NH _4^ + + 2H_2 O.$$ The latter reaction (b) was responsible for growth with nitrite. 2. Either succinate or fumarate could serve as sole carbon source during growth with nitrate or nitrite. Biosynthesis from succinate proceeded via fumarate. The ATP requirement for cell synthesis from succinate was equal to that calculated earlier for growth with fumarate as carbon source and electron acceptor (Brounder et al. 1982). 3. The cell yield at infinite dilution rate (Y max) as obtained with chemostat cultures was 8.5g dry cells/mol formate with either nitrate or nitrite as acceptor. This value amounts to 60% of that measured earlier with fumarate as acceptor (Mell et al. 1982). 4. Membrane vesicles prepared from V. succinogenes catalyzed electron transport from H2 to nitrate. The reaction was dependent on the menaquinone present in the membrane. 5. Electron transport with H2 and nitrite was coupled to the phosphorylation of ADP. The P/H2 ratio with nitrite was 40% of that measured with fumarate as acceptor using the same preparation. The phosphorylation but not the electron transport was abolished by an uncoupling agent.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-072X
    Keywords: Nitrite reductase ; Electron transport ; Wolinella succinogenes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Wolinella succinogenes grown with nitrate as terminal electron acceptor contains two nitrite reductases as measured with the donor viologen radical, one in the cytoplasm and the other integrated in the cytoplasmic membrane. The fumarate-grown bacteria contain only the membraneous species. The isolated membraneous enzyme consists of a single polypeptide chain (M r 63,000) carrying 4 hemeC groups and probably an iron-sulphur cluster as prosthetic groups. The enzyme amounts to about 1% of the total membrane protein. The isolated enzyme catalyses the reduction of nitrite to ammonium without accumulation of significant amounts of intermediates or alternative products. The Michaelis constant for nitrite was 0.1 mM and the turnover number of the hemeC 1.5 · 105 electrons per min at 37°C. The viologen-reactive site of the enzyme in the membrane is oriented towards the cytoplasm. When the isolated enzyme is incorporated into liposomes, the viologen-as well as the nitrite-reactive site is exposed to thooutside. The cytoplasmic membrane contains a second hemeC protein (M r 22,000) which may represent a cytochrome c.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 159 (1993), S. 491-497 
    ISSN: 1432-072X
    Keywords: Sulphur respiration ; Polysulphide ; Wolinella succinogenes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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