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  • 1
    Electronic Resource
    Electronic Resource
    Differentiation between Clostridium acidiurici and Clostridium cylindrosporum on the basis of specific metal requirements for formate dehydrogenase formation (1977)
    Springer
    Archives of microbiology 114 (1977), S. 219-224 
    Details
    ISSN: 1432-072X
    Keywords: Purine fermentation ; Formate dehydrogenase ; Tungsten ; Molybdenum ; Selenium ; Taxonomy ; Clostridium acidiurici ; Clostridium cylindrosporum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The formate dehydrogenases of Clostridium acidiurici and of C. cylindrosporum coupled the oxidation of formate with the reduction of viologen dyes. The basal activity level was about 0.85 μmoles/min s mg of protein for both species. The level of formate dehydrogenase of C. acidiurici increased 12-fold when 10-7 M tungstate and selenite were present during growth. Molybdate exerted no effect. On the other hand, molybdate and selenite were required to increase the formate dehydrogenase of C. cylindrosporum, and tungstate exhibited an antagonistic effect in this organism. Growth on hypoxanthine generally depended on the addition of bicarbonate. Supplementation with tungstate and selenite accelerated growth of C. acidiurici and increased again the level of formate dehydrogenase. The addition of both, molybdate and selenite was necessary to initiate growth of C. cylindrosporum and to form an active formate dehydrogenase. The differences in the requirement for metal ion supplementation to form high levels of formate dehydrogenase and their involvement in hypoxanthine degradation can be used to differentiate between C. acidiurici and C. cylindrosporum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446865
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  • 2
    Electronic Resource
    Electronic Resource
    Anaerobic degradation of uric acid via pyrimidine derivatives by selenium-starved cells of Clostridium purinolyticum (1982)
    Springer
    Archives of microbiology 131 (1982), S. 255-260 
    Details
    ISSN: 1432-072X
    Keywords: Purine fermentation ; Pyrimidines ; Selenium ; Clostridium purinolyticum ; HPLC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Clostridium purinolyticum decomposed uric acid via pyrimidine derivatives under selenium starvation conditions. Products were acetate, formate, glycine, ammonia, and CO2. 4,5-Diaminouracil could be identified as an intermediate after converting the labile substance into 6,7-dimethyllumazine. The breakdown of uric acid was inhibited by EDTA. High-pressure liquid chromatography methods have been developed for the simultaneous determination of uric acid, 4,5-diaminouracil, and 6,7-dimethyllumazine. The significance of the new pathway is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00405889
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  • 3
    Electronic Resource
    Electronic Resource
    Purification and characterization of threonine dehydrogenase from Clostridium sticklandii (1995)
    Springer
    Archives of microbiology 163 (1995), S. 286-290 
    Details
    ISSN: 1432-072X
    Keywords: Clostridium sticklandii ; Threonine dehydrogenase ; Aminoacetone ; Alcohol dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Threonine dehydrogenase from Clostridium sticklandii has been purified 76-fold from cells grown in a defined medium to a homogeneous preparation of 234 units · mg-1 protein. Purification was obtained by chromatography on Q-Sepharose fast flow and Reactive green 19-Agarose. The native enzyme had a molecular mass of 67 kDa and consisted of two identical subunits (33 kDa each). The optimum pH for catalytic activity was 9.0. Only l-threo-threo-nine, dl-β-hydroxynorvaline and acetoin were substrates; only NAD was used as the natural electron acceptor. The apparent K m values for l-threonine and NAD were 18 mM and 0.1 mM, respectively. Zn2+, Co2+ and Cu2+ ions (0.9 mM) inhibited enzyme activity. The N-terminal amino acid sequence revealed similarities to the class of non-metal short-chain alcohol dehydrogenases, whereas the threonine dehydrogenase from Escherichia coli belongs to the class of medium chain, zinc-containing alcohol dehydrogenases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00393382
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  • 4
    Electronic Resource
    Electronic Resource
    Molybdenum-dependent degradation of quinoline by Pseudomonas putida Chin IK and other aerobic bacteria (1991)
    Springer
    Archives of microbiology 155 (1991), S. 164-169 
    Details
    ISSN: 1432-072X
    Keywords: 2-Hydroxyquinoline ; Molybdenum-binding pterin ; Quinoline ; Quinoline dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Eighteen different aerobic bacteria were isolated which utilized quinoline as sole source of carbon, nitrogen, and energy. Attempts were unsuccessful at isolating anaerobic quinoline-degrading bacteria. The optimal concentration of quinoline for growth was in the range of 2.5 to 5 mM. Some organisms excreted 2-hydroxyquinoline as the first intermediate. Hydroxylation of quinoline was catalyzed by a dehydrogenase which was induced in the presence of quinoline or 2-hydroxyquinoline. Quinoline dehydrogenase activity was dependent on the availability of molybdate in the growth medium. Growth on quinoline was inhibited by tungstate, an antagonist of molybdate. Partially purified quinoline dehydrogenase from Pseudomonas putida Chin IK indicated the presence of flavin, iron-sulfur centers, and molybdenum-binding pterin. M r of quinoline dehydrogenase was about 300 kDa in all isolates investigated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00248612
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  • 5
    Electronic Resource
    Electronic Resource
    The effect of ferrous ions, tungstate and selenite on the level of formate dehydrogenase inClostridium formicoaceticum and formate synthesis from CO2 during pyruvate fermentation (1974)
    Springer
    Archives of microbiology 96 (1974), S. 103-118 
    Details
    ISSN: 1432-072X
    Keywords: Clostridium formicoaceticum ; Formate Dehydrogenase ; CO2 Reduction ; Pyruvate Fermentation ; Tungstate ; Selenite ; Molybdate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In a medium containing a trace element solution and 10-4 M ferrous ions the growth yield ofClostridium formicoaceticum on fructose was 5.5 g of weight per l; in the absence of metal ion solution it was 1 g per l. The specific activity of methyl viologen dependent formate dehydrogenase under both conditions was 0.28 and 0.03 units per mg of protein, respectively. It could be increased to 9.75 units when the growth medium contained 10-4 M tungstate and 10-5 M selenite in addition. Molybdate was only about 40% as effective as tungstate. Tungstate or molybdate could not be replaced by vanadate, selenite not by sulfide. The formate dehydrogenase catalyzed also the reduction of CO2 to formate. The highest rate of formate synthesis was observed when pyruvate served as the reductant. No pyruvate: formate exchange but rapid pyruvate: CO2 exchange could be observed with cell-free extracts ofC. formicoaceticum. Pyruvate is fermented byC. formicoaceticum to yield up to 1.16 mole acetate per mole of pyruvate. Resting cells accumulated some formate in addition to acetate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00590167
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  • 6
    Electronic Resource
    Electronic Resource
    Some properties of formate dehydrogenase, accumulation and incorporation of 185W-tungsten into proteins of Clostridium formicoaceticum (1977)
    Springer
    Archives of microbiology 115 (1977), S. 277-284 
    Details
    ISSN: 1432-072X
    Keywords: Clostridium formicoaceticum ; Formate dehydrogenase ; Tungsten uptake ; Tungstoproteins ; Molybdenum ; Selenium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Formate dehydrogenase of Clostridium formicoaceticum used only methyl and benzyl viologen, but not NAD as electron acceptor. The S0.5 values were 0.9×10-4 M for formate and 5.8×10-3 M for methyl viologen. Using potassium phosphate buffer a pH-optimum of 7.9 was observed. The initial velocity of the formate dehydrogenase activity reached a maximum at 70°C, whereas the activity was stable only up to 50°C. The level of formate dehydrogenase in C. formicoaceticum was increased to its maximum when 10-6 M selenite and 10-7 M tungstate were added to a synthetic medium. Addition of molybdate instead of tungstate did not increase the level of formate dehydrogenase. 185W-tungsten was concentrated about 100-fold by C. formicoaceticum; molybdate had no major effect on the uptake of tungsten. 185W-tungsten was found almost exclusively in the soluble fluid and was predominantly recovered after chromatography in a protein of about 88000 molecular weight. Occasionally a labelled protein of low molecular weight was observed. Again molybdate added even in high molar excess did not influence the labelling pattern. No radioactivity peak could be obtained at the elution peak of formate dehydrogenase activity. The extreme instability of formate dehydrogenase prevented further purification.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446453
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  • 7
    Electronic Resource
    Electronic Resource
    Glycine fermentation via a glycine reductase in Peptococcus glycinophilus and Peptococcus magnus (1983)
    Springer
    Archives of microbiology 134 (1983), S. 127-135 
    Details
    ISSN: 1432-072X
    Keywords: Peptococcus glycinophilus ; Peptococcus magnus ; Glycine fermentation ; Glycine reductase ; Selenium ; CO2 reduction to acetate ; B12 content ; CO dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Peptococcus glycinophilus and P. magnus (P. variabilis) utilized only glycine-containing compounds for growth and required selenium compounds for the fermentation of glycine in an optimized medium. Under these conditions an active glycine reductase was expressed in vivo as demonstrated for both species by tracer experiments and additionally in vitro for P. glycinophilus in cell extracts. It is concluded that the availability of selenium determines the fermentation pathway of glycine. In the presence of selenite glycine is converted via the glycine reductase rather than the hitherto known glycine-serine-pyruvate interconversion. The molar growth yield of P. magnus was determined to be 8.9 g of dry weight per mol of glycine. The significance of the low vitamin B12 content and a low carbon monoxide dehydrogenase activity in P. glycinophilus for the reduction of CO2 to acetate is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00407945
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  • 8
    Electronic Resource
    Electronic Resource
    Aerobic and anaerobic degradation of furan-3-carboxylate by Paracoccus denitrificans strain MK33 (1991)
    Springer
    Archives of microbiology 157 (1991), S. 70-75 
    Details
    ISSN: 1432-072X
    Keywords: Furan-3-carboxylate oxygenase ; 3-Furoyl-CoA reductase ; Paracoccus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An organism identified as Paracoccus denitrificans was isolated from an enrichment culture with furan-3-carboxylate as its sole source of carbon and energy. The organism degraded furan-3-carboxylate under aerobic and — in the presence of nitrate - under anaerobic conditions. The aerobic degradation was initiated by an oxygenase reaction to form probably 2-hydroxy-3-furoate. Under anaerobic conditions the first intermediate was 3-furoyl-CoA which was reduced by NADPH to probably 4,5-dihydro-furoyl-CoA. Succinic semialdehyde was an intermediate in both aerobic and anaerobic mechanism of furan-3-carboxylate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245338
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  • 9
    Electronic Resource
    Electronic Resource
    Peptostreptococcus barnesae sp. nov., a Gram-positive, anaerobic, obligately purine utilizing coccus from chicken feces (1985)
    Springer
    Archives of microbiology 143 (1985), S. 26-31 
    Details
    ISSN: 1432-072X
    Keywords: Peptostreptococcus barnesae ; Intestinal bacteria ; Anaerobic cocci of Hare group IX ; Purine metabolism ; Glycine metabolism ; Selenium ; Molybdenum ; Tungsten
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Anaerobic, Gram-positive cocci were obtained from chicken feces by direct isolation, which grew on the purines uric acid, xanthine, 6,8-dihydroxypurine, guanine, and hypoxanthine. Adenine and glycine were fermented, but not as readily. Acetate, formate, ammonia, and CO2 were products. The isolated strains were nutritionally non-fastidious, however, they required selenite, molybdate, and tungstate as micronutrients. The cells were spherical and 0.5–0.9 μm in diameter. The addition of bile salts enhanced the growth rate in most cases. The organisms proved to be quite resistant to lysis. The guanosine-plus-cytosine (G+C) content of their deoxyribonucleic acid was 33.6 to 34.8 mol%. The peptidoglycan was of the same structure (Gly-Lys-d-Asp) as reported for the anaerobic cocci of Hare group IX. However, the latter strains could only utilize glycine, not purines. Therefore, it is proposed to form a new species, Peptostreptococcus barnesae sp. nov.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414763
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  • 10
    Electronic Resource
    Electronic Resource
    Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini (1990)
    Springer
    Archives of microbiology 154 (1990), S. 605-613 
    Details
    ISSN: 1432-072X
    Keywords: Bacillus niacini ; Bactopterin ; 6-Hydroxynicotinate dehydrogenase ; Molybdenum ; Nicotinate dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The enzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini could be purified to homogeneity by means of anion exchange chromatography, hydrophobic interaction chromatography, gel filtration, and chromatography on hydroxylapatite. During enrichment procedures both enzymes showed a significant loss in specific activity. The molecular weight of nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase was determined to be about 300,000 and 120,000, respectively. They were highly substrate specific and transferred electrons only to artificial acceptors of high redox potential. The K m for their specific substrates was about 1.0 mM for both enzymes, and their pH optimum was determined to be 7.5. For nicotinate dehydrogenase a content of 8.3 mol iron, 1.5 mol acid-labile sulfur, 2.0 mol flavin, and 1.5 mol molybdenum per mol of enzyme was determined. Both enzymes contained FAD and Fe/S center. After inhibition by KCN, thiocyanate was detected, and subsequently the initial nicotinate dehydrogenase activity was restored by the addition of Na2S indicating the presence of cyanolyzable sulfur. 6-Hydroxynicotinate dehydrogenase seemed to contain the same type of constituents as determined for nicotinate dehydrogenase. A partial immunological identity of the enzymes could be shown by antibodies raised against nicotinate dehydrogenase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00248844
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