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  • 1
    Electronic Resource
    Electronic Resource
    Competition between the facultatively chemolithotrophic Thiobacillus A2, an obligately chemolithotrophic Thiobacillus and a heterotrophic spirillum for inorganic and organic substrates (1979)
    Springer
    Archives of microbiology 121 (1979), S. 241-249 
    Details
    ISSN: 1432-072X
    Keywords: Thiobacillus A2 ; Mixotrophy ; Competition ; Mixed cultures ; Facultative chemolithotroph ; Ecological niche
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Competition in a chemostat between the versatile Thiobacillus A2 and the specialized T. neapolitanus for thiosulfate as the sole growth-limiting substrate, led to dominance of the specialized over the versatile organism, at dilution rates ≥0.025 h-1. Increasing concentrations of acetate or glycollate in the thiosulfate medium caused increased relative numbers of T. A2 in steady states at D=0.07 h-1. Eventually, with 10–12 mmol of organic substrate per litre, complete dominance of T. A2 over T. neapolitanus occurred. Mixed cultures of T. A2 and a specialized spirillumshaped heterotroph, competing for acetate as sole growth-limiting substrate resulted in complete dominance of the heterotroph at dilution rates of 0.07 and 0.15 h-1. In this case increasing concentrations of thiosulfate in the acetate medium, up to 10 mM, eventually led to the elimination of the heterotroph. These results have been interpreted as evidence that T. A2 was growing mixotrophically. As the concentration of the second substrate was raised, the number of T. A2 cells increased and as a result T. A2 consumed an increasing portion of the common substrate. In mixed chemostat cultures containing all three organisms, T. A2 could maintain itself with all tested ratios of acetate and thiosulfate in the inflowing medium. The heterotroph was excluded from the culture below a relatively low acetate to thiosulfate ratio, whilst above a relatively high acetate to thiosulfate ratio T. neapolitanus was completely eliminated. These results were discussed in relation to the ecological niche of Thiobacillus A2-type organisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425062
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  • 2
    Electronic Resource
    Electronic Resource
    Metabolic flexibility of Thiobacillus A 2 during substrate transitions in the chemostat (1981)
    Springer
    Archives of microbiology 129 (1981), S. 23-28 
    Details
    ISSN: 1432-072X
    Keywords: Thiobacillus A 2 ; Mixotrophy ; Enzyme-induction ; Enzyme-inactivation ; Metabolic flexibility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract During autotrophic growth, cells of Thiobacillus A 2 retained a considerable capacity to oxidize various organic energy sources. Heterotrophically grown cultures, on the other hand, were completely devoid of the capacity to fix CO2 via the Calvin cycle and to generate energy from thiosulfate. During transitions from organic media to inorganic thiosulfate-containing media in the chemostat, a long lag-phase was observed before energy generation, CO2 fixation and, consequenctly, measurable growth occurred. This lag-phase was practically abolished if substrates were presentm at very low concentrations in the thiosulfate mineral medium which could be used as an energy source. The same result was obtained when the cells contained reserve material at the moment of the transition. During transitions from thiosulfate-limited growth to starvation, the $${\text{Q}}_{{\text{O}}_{\text{2}} }^{{\text{max}}} $$ -thiosulfate and the capacity to fix CO2 decreased very slowly, after an initial short (± 4 h) increase of both enzyme systems. In contrast, these two metabolic functions were inactivated relatively rapidly in the presence of an oxidizable organic carbon and energy source. This process of inactivation was instantaneously stopped and reversed into rapid enzyme synthesis upon replacement of the organic substrate by thiosulfate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00417173
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  • 3
    Electronic Resource
    Electronic Resource
    Aerobic denitrification: a controversy revived (1984)
    Springer
    Archives of microbiology 139 (1984), S. 351-354 
    Details
    ISSN: 1432-072X
    Keywords: Aerobic denitrification ; Thiosphaera pantotropha ; Nitrate reduction ; Bacterial selection ; Ecology ; Oxygen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract During studies on the denitrifying mixotroph, Thiosphaera pantotropha, it has been found that this organism is capable of simultaneously utilizing nitrate and oxygen as terminal electron acceptors in respiration. This phenomenon, termed aerobic denitrification, has been found in cultures maintained at dissolved oxygen concentrations up to 90% of air saturation. The evidence for aerobic denitrification was obtained from a number of independant experiments. Denitrifying enzymes were present even in organisms growing aerobically without nitrate. Aerobic yields on acetate were higher (8.1 g protein/mol) without than with (6.0 g protein/mol) nitrate, while the anaerobic yield with nitrate was even lower (4 g protein/mol). The maximum specific growth rate of Tsa. pantotropha was higher (0.34 h-1) in the presence of both oxygen (〉80% air saturation) and nitrate than in similar cultures not supplied with nitrate (0.27 h-1), indicating that the rate of electron transport to oxygen was limiting. This was confirmed by oxygen uptake experiments which showed that although the rate of respiration on acetate was not affected by nitrate, the total oxygen uptake was reduced in its presence. The original oxygen uptake could be restored by the addition of denitrification inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408378
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  • 4
    Electronic Resource
    Electronic Resource
    Purification and characterization of a periplasmic thiosulfate dehydrogenase from the obligately autotrophicThiobacillus sp. W5 (1996)
    Springer
    Archives of microbiology 166 (1996), S. 372-378 
    Details
    ISSN: 1432-072X
    Keywords: Thiobacilli ; Chemolithoautotrophy ; Thiosulfate dehydrogenase ; Thiosulfate ; Tetrathionate ; Cytochromec ; Respiratory chain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A periplasmic thiosulfate dehydrogenase (EC 1.8.2.2) was purified to homogeneity from the neutrophilic, obligately chemolithoautotrophicThiobacillus sp. W5. A five-step procedure resulted in an approximately 2,300-fold purification. The purified protein had a molecular mass of 120±3 kDa, as determined by gel filtration. It is probably a tetramer containing two different subunits with molecular masses of 33±1 kDa and 27±0.5 kDa, as determined by SDS-PAGE. UV/visible spectroscopy revealed that the enzyme contained haemc; haem staining showed that both subunits contained haemc. A haemc content of 4 mol per mol of enzyme was calculated using the pyridine haemochrome test. The pH optimum of the enzyme was 5.5 At pH 7.5, the Km and Vmax were 120±10 μM and 1,160±30 U mg-1, respectively. The absence of 2-heptyl-4-hydroquinoline-N-oxide (HQNO) inhibition for the oxidation of thiosulfate by whole cells suggested that the electrons enter the respiratory chain at the level of cytochromec. Comparison with thiosulfate dehydrogenases from otherThiobacillus species showed that the enzyme was structurally similar to the thiosulfate dehydrogenase of the acidophilic, facultatively chemolithoautotrophicThiobacillus acidophilus, but not to the thiosulfate dehydrogenases published for the obligately chemolithoautotrophicThiobacillus tepidarius andThiobacillus thioparus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01682982
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  • 5
    Electronic Resource
    Electronic Resource
    Mixotrophic growth of Thiobacillus A2 on acetate and thiosulfate as growth limiting substrates in the chemostat (1980)
    Springer
    Archives of microbiology 126 (1980), S. 33-42 
    Details
    ISSN: 1432-072X
    Keywords: Thiobacillus A2 ; Mixotrophic growth ; Facultatively chemolithotrophic Thiobacillus ; Dual substrate limitation ; Assimilation efficiency
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract During heterotrophic growth on acetate, in batch culture, the autotrophic growth potential of Thiobacillus A2, i.e. the capacity to oxidize thiosulfate and to fix carbon dioxide via the Calvin cycle, was completely repressed. The presence of thiosulfate in a batch culture with acetate as the organic substrate partly released the repression of the thiosulfate oxidizing system. Cultivation of the organism in continuous culture at a dilution rate of 0.05 h-1 with different concentration ratios of thiosulfate and acetate in the reservoir medium led to mixotrophic growth under dual substrate limitation. Growth on the different mixtures of acetate and thiosulfate yielded upto 30% more cell dry weight than predicted from the growth yields on comparable amounts of these substrates separately. The extent to which the carbon dioxide fixation capacity and the maximum thiosulfate and acetate oxidation capacity are repressed appeared to be a function of the thiosulfate to acetate concentration ratio in the reservoir medium. The results of 14C-acetate assimilation experiments and of gas-analysis demonstrated that the extent to which acetate was assimilated depended also on the substrate ratio in the inflowing medium. Under the different growth conditions surprisingly little variation was found in some tri-carboxylic acid cycle enzyme activities. Cultivation of T. A2 at different growth rates with a fixed mixture of thiosulfate (18 mM) and acetate (11 mM) in the medium, showed that dual substrate limitation occured at dilution rates ranging from 0.03–0.20 h-1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00421888
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  • 6
    Electronic Resource
    Electronic Resource
    A novel membrane-bound flavocytochrome c sulfide dehydrogenase from the colourless sulfur bacterium Thiobacillus sp. W5 (1997)
    Springer
    Archives of microbiology 167 (1997), S. 295-301 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsThiobacillus sp. W5 ; Sulfide oxidation ; Sulfur formation ; Flavocytochrome c ; Chlorobium ; limicola ; Chromatium vinosum ; Thiobacilli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A novel membrane-bound sulfide-oxidizing enzyme was purified 102-fold from the neutrophilic, obligately chemolithoautotrophic Thiobacillus sp. W5 by means of a six-step procedure. Spectral analysis revealed that the enzyme contains haem c and flavin. SDS-PAGE showed the presence of two types of subunit with molecular masses of 40 and 11 kDa. The smaller subunit contains covalently bound haem c, as was shown by haem staining. A combination of spectral analysis and the pyridine haemochrome test indicated that the sulfide-oxidizing heterodimer contains one molecule of haem c and one molecule of flavin. It appeared that the sulfide-oxidizing enzyme is a member of a small class of redox proteins, the flavocytochromes c, and is structurally most related to the flavocytochrome c sulfide dehydrogenase of the green sulfur bacterium Chlorobium limicola. The pH optimum of the enzyme is 8.6. At pH 9, the V max was 2.1 ± 0.1 μmol cytochrome c (mg protein)–1 min–1, and the K m values for sulfide and cytochrome c were 1.7 ± 0.4 μM and 3.8 ± 0.8 μM, respectively. Cyanide inhibited the enzyme by the formation of an N-5 adduct with the flavin moiety of the protein. On the basis of electron transfer stoichiometry, it seems likely that sulfur is the oxidation product.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050447
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  • 7
    Electronic Resource
    Electronic Resource
    Protein composition of the carboxysomes of Thiobacillus neapolitanus (1986)
    Springer
    Archives of microbiology 144 (1986), S. 398-404 
    Details
    ISSN: 1432-072X
    Keywords: Carboxysomes ; Polyhedral bodies ; Protein composition ; Ribulose-1,5-bisphosphate carboxylase ; Shell glycoproteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract For purifying carboxysomes of Thiobacillus neapolitanus an isolation procedure was developed which resulted in carboxysomes free from whole cells, protoplasts and cell fragments. These purified carboxysomes are composed of 8 proteins and at the most of 13 polypeptides. The two most abundant proteins which make up more than 60% of the carboxysomes, are ribulose-1,5-bisphosphate carboxylase and a glycoprotein with a molecular weight of 54,000. The shell of the carboxysomes consists of four glycoproteins, one also with a molecular weight of 54,000. The other proteins are present in minor quantities. Ribulose-1,5-bisphosphate carboxylase is the only enzyme which could be detected in the carboxysomes and 3-phosphoglycerate was the only product formed during incubation with ribulose-1,5-diphosphate and bicarbonate. The supernatant of a broken and centrifuged carboxysome suspension contained the large subunit of ribulose-1,5-bisphosphate carboxylase. The small subunit of ribulose-1,5-bisphosphate carboxylase was found in the pellet together with the shell proteins which indicates that the small subunit of ribulose-1,5-bisphosphate carboxylase is connected to the shell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409891
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  • 8
    Electronic Resource
    Electronic Resource
    Oxidation of reduced sulphur compounds by intact cells of Thiobacillus acidophilus (1992)
    Springer
    Archives of microbiology 157 (1992), S. 161-168 
    Details
    ISSN: 1432-072X
    Keywords: Thiobacillus acidophilus ; Acidophiles ; Sulphur metabolism ; Sulphide ; Elemental sulphur ; Thiosulphate ; Tetrathionate ; Trithionate ; Sulphite ; Hydrolytic polythionate cleavage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Oxidation of reduced sulphur compounds by Thiobacillus acidophilus was studied with cell suspensions from heterotrophic and mixotrophic chemostat cultures. Maximum substrate-dependent oxygen uptake rates and affinities observed with cell suspensions from mixotrophic cultures were higher than with heterotrophically grown cells. ph Optima for oxidation of sulphur compounds fell within the pH range for growth (pH 2–5), except for sulphite oxidation (optimum at pH 5.5). During oxidation of sulphide by cell suspensions, intermediary sulphur was formed. Tetrathionate was formed as an intermediate during aerobic incubation with thiosulphate and trithionate. Whether or not sulphite is an inter-mediate during sulphur compound oxidation by T. acidophilus remains unclear. Experiments with anaerobic cell suspensions of T. acidophilus revealed that trithionate metabolism was initiated by a hydrolytic cleavage yielding thiosulphate and sulphate. A hydrolytic cleavage was also implicated in the metabolism of tetrathionate. After anaerobic incubation of T. acidophilus with tetrathionate, the substrate was completely converted to equimolar amounts of thiosulphate, sulphur and sulphate. Sulphide- and sulphite oxidation were partly inhibited by the protonophore uncouplers 2,4-dinitrophenol (DNP) and carbonyl cyanide m-chlorophenylhydrazone (CCCP) and by the sulfhydryl-binding agent N-ethylmaleimide (NEM). Oxidation of elemental sulphur was completely inhibited by these compounds. Oxidation of thiosulphate, tetrathionate and trithionate was only slightly affected. The possible localization of the different enzyme systems involved in sulphur compound oxidation by T. acidophilus is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245285
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  • 9
    Electronic Resource
    Electronic Resource
    Purification and characterization of a periplasmic thiosulfate dehydrogenase from the obligately autotrophic Thiobacillus sp. W5 (1997)
    Springer
    Archives of microbiology 166 (1997), S. 372-378 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsThiobacilli ; Chemolithoautotrophy ; Thiosulfate dehydrogenase ; Thiosulfate ; Tetrathionate ; Cytochrome c ; Respiratory chain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A periplasmic thiosulfate dehydrogenase (EC 1.8.2.2) was purified to homogeneity from the neutrophilic, obligately chemolithoautotrophic Thiobacillus sp. W5. A five-step procedure resulted in an approximately 2,300-fold purification. The purified protein had a molecular mass of 120 ± 3 kDa, as determined by gel filtration. It is probably a tetramer containing two different subunits with molecular masses of 33 ± 1 kDa and 27 ± 0.5 kDa, as determined by SDS-PAGE. UV/visible spectroscopy revealed that the enzyme contained haem c; haem staining showed that both subunits contained haem c. A haem c content of 4 mol per mol of enzyme was calculated using the pyridine haemochrome test. The pH optimum of the enzyme was 5.5. At pH 7.5, the Km and Vmax were 120 ± 10 μM and 1,160 ± 30 U mg–1, respectively. The absence of 2-heptyl-4-hydroquinoline-N-oxide (HQNO) inhibition for the oxidation of thiosulfate by whole cells suggested that the electrons enter the respiratory chain at the level of cytochrome c. Comparison with thiosulfate dehydrogenases from other Thiobacillus species showed that the enzyme was structurally similar to the thiosulfate dehydrogenase of the acidophilic, facultatively chemolithoautotrophic Thiobacillus acidophilus, but not to the thiosulfate dehydrogenases published for the obligately chemolithoautotrophic Thiobacillus tepidarius and Thiobacillus thioparus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01682982
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  • 10
    Electronic Resource
    Electronic Resource
    Growth of Nitrosomonas europaea on hydroxylamine (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 125 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Hydroxylamine is an intermediate in the oxidation of ammonia to nitrite, but until now it has not been possible to grow Nitrosomonas europaea on hydroxylamine. This study demonstrates that cells of N. europaea are capable of growing mixotrophically on ammonia and hydroxylamine. The molar growth yield on hydroxylamine (4.74 g mol−1 at a growth rate of 0.03 h−1) was higher than expected. Aerobically growing cells of N. europaea oxidized ammonia to nitrite with little loss of inorganic nitrogen, while significant inorganic nitrogen losses occurred when cells were growing mixotrophically on ammonia and hydroxylamine. In the absence of oxygen, hydroxylamine was oxidized with nitrite as electron acceptor, while nitrous oxide was produced. Anaerobic growth of N. europaea on ammonium, hydroxylamine and nitrite could not be observed at growth rates of 0.03 h−1 and 0.01 h−1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07355.x
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