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  • Chemolithoautotrophy
  • Springer  (7)
  • Nature Publishing Group  (1)
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  • Springer  (7)
  • Nature Publishing Group  (1)
  • 1
    Publication Date: 2022-05-26
    Description: © The Author(s), 2012. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in The ISME Journal 6 (2012): 1901-1915, doi:10.1038/ismej.2012.31.
    Description: Antarctic surface oceans are well-studied during summer when irradiance levels are high, sea ice is melting and primary productivity is at a maximum. Coincident with this timing, the bacterioplankton respond with significant increases in secondary productivity. Little is known about bacterioplankton in winter when darkness and sea-ice cover inhibit photoautotrophic primary production. We report here an environmental genomic and small subunit ribosomal RNA (SSU rRNA) analysis of winter and summer Antarctic Peninsula coastal seawater bacterioplankton. Intense inter-seasonal differences were reflected through shifts in community composition and functional capacities encoded in winter and summer environmental genomes with significantly higher phylogenetic and functional diversity in winter. In general, inferred metabolisms of summer bacterioplankton were characterized by chemoheterotrophy, photoheterotrophy and aerobic anoxygenic photosynthesis while the winter community included the capacity for bacterial and archaeal chemolithoautotrophy. Chemolithoautotrophic pathways were dominant in winter and were similar to those recently reported in global ‘dark ocean’ mesopelagic waters. If chemolithoautotrophy is widespread in the Southern Ocean in winter, this process may be a previously unaccounted carbon sink and may help account for the unexplained anomalies in surface inorganic nitrogen content.
    Description: CSR was supported by an NSF Postdoctoral Fellowship in Biological Informatics (DBI-0532893). The research was supported by National Science Foundation awards: ANT 0632389 (to AEM and JJG), and ANT 0632278 and 0217282 (to HWD), all from the Antarctic Organisms and Ecosystems Program.
    Keywords: Antarctic bacterioplankton ; Metagenomics ; Chemolithoautotrophy
    Repository Name: Woods Hole Open Access Server
    Type: Article
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 160 (1993), S. 152-157 
    ISSN: 1432-072X
    Keywords: Thiothrix ramosa ; Chemolithoautotrophy ; Chemostat ; Ribulose bisphosphate carboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Thiothrix has been shown for the first time to be able to grow chemolithoautotrophically with thiosulphate or carbon disulphide as sole energy substrate. Thiosulphate served as the growth-limiting substrate for Thiothrix ramosa in chemostat culture. Maximum growth yield (Ymax) from yields at growth rates between 0.029–0.075 h-1 was 4.0 g protein/mol thiosulphate oxidized. The key enzyme of the Calvin cycle, ribulose 1,5-bisphosphate carboxylase, was present in these cells, as were rhodanese, adenylyl sulphate (APS) reductase and ‘sulphur-oxidizing enzyme’. Thiosulphate-grown cells oxidized thiosulphate, sulphide, tetrathionate and carbon disulphide. Oxidation kinetics for sulphide, thiosulphate and tetrathionate were biphasic: oxygen consumption during the fast first phase of oxidation indicated oxidation of sulphide, and the sulphane moieties of thiosulphate and tetrathionate, to elemental sulphur, before further oxidation to sulphate. Kinetic constants for these four substrates were determined. T. ramosa also grew mixotrophically in batch culture on lactate with a number of organic sulphur compounds: carbon disulphide, methanethiol and diethyl sulphide. Substituted thiophenes were also used as sole substrates. The metabolic versatility of T. ramosa is thus much greater than previously realised.
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  • 3
    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.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 116 (1978), S. 221-229 
    ISSN: 1432-072X
    Keywords: Aquaspirillum autotrophicum ; Hydrogen bacterium ; Growth ; Chemolithoautotrophy ; Particulate hydrogenase ; Induction ; Repression ; Natural habitats
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Aquaspirillum autrotrophicum, an aerobic hydrogen bacterium recently isolated from an eutrophic freshwater lake, was characterized physiologically. It grew autotrophically in a fermenter with a doubling time of 4 h. Heterotrophic growth was faster. pH-Optimum ranged from 5.0–7.5, temperature optimum was about 28° C. During autotrophic growth about 10 moles hydrogen were consumed per 1 mole carbon dioxide fixed. Hydrogenase activity is inducible. CO2 did not enhance the oxy-hydrogen reaction by intact cells. The hydrogenase activity was localized in the particulate fraction. The hydrogenase reduced methylene blue and phenazine methosulfate; pyridine nucleotides were not reduced. In cell-free extracts, hydrogenase was sensitive to oxygen. Ribulosebisphosphate carboxylase was present in autotrophically-grown cells and absent from heterotrophically grown cells. Hydrogenase induction in heterotrophically-grown cells followed parabolic kinetics. Oxygen and D-gluconate repressed hydrogenase synthesis, whereas citrate, DL-lactate and pyruvate stimulated its formation. The repressive effect was delayed. The results suggest that the control of hydrogenase synthesis occurred at the transcriptional level, and that mRNA coding for the hydrogenase had a relatively long life span. D-Gluconate was degraded via the Entner-Doudoroff pathway, the enzymes of which were constitutively formed. Enzymes of the pentosephosphate and Embden-Meyerhof pathways (except phosphofructokinase) were present, too. Hydrogen did not inhibit heterotrophic growth. The possible competitive advantage of the physiological properties described with regard to the natural habitat was discussed.
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  • 5
    ISSN: 1432-072X
    Keywords: Chromatiaceae ; Chlorobiaceae ; Thiocystis violacea ; Chromatium vinosum ; Chemolithoautotrophy ; Mixotrophy ; Specific respiration rates ; Growth yields
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The capacity for chemoautotrophic, mixotrophic and organotrophic growth in the dark was tested with 45 strains of 17 species (11 genera) of the Chromatiaceae. The auxanographic deep agar shake culture method was used; the gas phase contained 5% O2 and 1% CO2 in N2. All strains tested of Chromatium vinosum, C. minus, C. violascens, C. gracile, Thiocystis violacea, Amoebobacter roseus, Thiocapsa roseopersicina gave positive growth responses under chemoautotrophic and mixotrophic conditions (extra carbon source acetate); one strain of Thiocapsa roseopersicina grew also organotrophically on acetate alone. No growth was obtained with the remaining 17 strains of ten species. None of the five type species (three genera) of the Chlorobiaceae grew under chemotrophic conditions. With Thiocystis violacea 2311 a growth yield of 11.3g dry weight per mol thiosulfate consumed was obtained under chemoautotrophic conditions; under mixotrophic conditions with acetate the yield increased to 69g dry weight per mol thiosulfate consumed. With Thiocystis violacea 2311 maximal specific respiration rates were obtained with thiosulfate as electron donor irrespective of the presence or absence of sulfur globules in the cells; organic substrates served as carbon sources only and did not support respiration. With Chromatium vinosum D utilization of thiosulfate was not constitutive; maximal respiration rates on thiosulfate were obtained only with thiosulfate grown cells containing sulfur globules. Respiration rates were further increased by malate, fumarate or propionate; these substrates also served as sole electron donors for respiration. Acetate and pyruvate were used as carbon sources only. The ecological significance of the chemotrophic metabolism is discussed.
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  • 6
    ISSN: 1432-072X
    Keywords: Bacillus tusciae ; New species ; Taxonomy ; Ecology ; Chemolithoautotrophy ; Hydrogen oxidation ; Hydrogenase ; Thermophily ; Geothermal manifestation ; Solfatara
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A thermophilic, chemolithoautotrophic, hydrogen-oxidizing sporeformer has been isolated from ponds in a solfatara in the geothermal area of Tuscany (Italy). Some physicochemical parameters of the habitat were determined. The habitat was characterized by the presence of molecular hydrogen in the escaping gases, a very low content of phosphate and organic matter. Temperature and water level in the ponds varied widely. The organism formed oval, subterminal spores, which swelled distinctly the sporangium. Optimal growth occured between pH 4.2 and 4.8 at 55°C. It grew best under autotrophic conditions, but organic substrates including short chain fatty acids, amino acids and alcohols could also support heterotrophic growth. Sugars were not metabolized. The hydrogenase was soluble but did not reduce pyridine nucleotides. Based on its morphological and biochemical features, the organism belongs to the genus Bacillus, but differs from all the previously described species. It is therefore proposed as constituting a new species, Bacillus tusciae.
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  • 7
    ISSN: 1432-072X
    Keywords: Gallionella ferruginea ; Thiobacillus ferrooxidans ; Iron bacteria ; Chemolithoautotrophy ; Ultrastructure ; Freeze-etching ; Cell wall organization ; Intracytoplasmic membranes ; Carboxysomes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract By using sodium thioglycolate to dissolve the high amount of excreted stalk material in axenic cultures of the chemolithoautotrophic iron bacterium Gallionella ferruginea, the ultrastructure of Gallionella cells from pure cell suspensions could be studied without any loss of viability or disturbance by dense ferric stalk fibers, and compared with Thiobacillus ferrooxidans, also grown chemolithoautotrophically with ferrous iron as energy source. Both organisms were chemically fixed or freeze-etched. Particular structural differences between these iron-bacteria could be ascertained. G. ferruginea possesses intracytoplasmic membranes and soluble d-ribulose-1,5-bisphosphate-carboxylase, whereas T. ferrooxidans contains carboxysomes but no intracytoplasmic membranes; Gallionella forms poly-β-hydroxybutyrate and glycogen as storage material; T. ferrooxidans produces only glycogen. Both organisms also differ from each other with respect to the freeze fracture behaviour of the cell envelope layers. Whereas the cells of T. ferrooxidans exhibit a characteristic double cleavage, exposing the plasmic fracture face and exoplasmic fracture face of the outer membrane and cytoplasmic membrane, the exceptionally thin multilayered cell envelope of G. ferruginea revealed a particularly intimate association between the layers, resulting in a visualisation of the supramolecular organisation of only the inner fracture face of the cytoplasmic membrane. The results are discussed predominantly in relation to the extremely distinct environments of both organisms.
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  • 8
    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.
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