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  • 11
    ISSN: 1432-072X
    Keywords: Nitrification ; Hydroxylamine-cytochromec oxidoreductase ; Ammonia monooxygenase ; Denitrification ; Pseudomonas sp.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Hydroxylamine oxidation was measured in four recently isolated heterotrophic nitrate-reducing bacteria belonging to the generaPseudomonas, Moraxella, Arthrobacter andAeromonas. A hydroxylamine-cytochromec oxidoreductase activity was detected in periplasmic fractions of thePseudomonas andAeromonas spp. and in total soluble fractions of theArthrobacter sp. A monomeric 19-kDa non-haem iron hydroxylamine-cytochromec oxidoreductase was purified from thePseudomonas species and shown to be similar to hydroxylaminecytochromec oxidoreductase ofParacoccus denitrificans.
    Type of Medium: Electronic Resource
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  • 12
    ISSN: 1432-072X
    Keywords: Key words Nitrification ; Hydroxylamine-cytochrome c oxidoreductase ; Ammonia monooxygenase ; Denitrification ; Pseudomonas sp.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Hydroxylamine oxidation was measured in four recently isolated heterotrophic nitrate-reducing bacteria belonging to the genera Pseudomonas, Moraxella, Arthrobacter and Aeromonas. A hydroxylamine-cytochrome c oxidoreductase activity was detected in periplasmic fractions of the Pseudomonas and Aeromonas spp. and in total soluble fractions of the Arthrobacter sp. A monomeric 19-kDa non-haem iron hydroxylamine-cytochrome c oxidoreductase was purified from the Pseudomonas species and shown to be similar to hydroxylamine-cytochrome c oxidoreductase of Paracoccus denitrificans.
    Type of Medium: Electronic Resource
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  • 13
    ISSN: 1432-072X
    Keywords: Denitrification ; Pseudomonas putida ; Nitrate reductase ; Periplasm ; Aerobic nitrate respiration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A strain of Pseudomonas putida that can express a nitrate reductase that is located in the periplasmic compartment was isolated from freshwater. The enzyme was active in vivo during arginine fermentation and at the onset of oxygen limitation in batch cultures. The activity of the enzyme increased the yield of bacteria following fermentative growth under anoxic conditions with arginine, but nitrate reduction did not support growth on nonfermentable carbon substrates under anoxic conditions. Cells expressing the periplasmic nitrate reductase were capable of reducing nitrate in the presence of oxygen. Nitrate reduction under oxic conditions was clearly coupled to a respiratory electron transport chain because: (1) the process was sensitive to the respiratory inhibitors rotenone and 2-n-heptyl-4-hydroxyquinoline N-oxide, and (2) membrane-bound and periplasmic cytochromes were involved. This is the first report of the presence of a periplasmic nitrate reductase in a member of the γ proteobacteria.
    Type of Medium: Electronic Resource
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  • 14
    ISSN: 1432-072X
    Keywords: Key words Nitrate assimilation ; Nitrate reductase ; Paracoccus denitrificans ; Thiosphaera pantotropha
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A Paracoccus denitrificans strain (M6Ω) unable to use nitrate as a terminal electron acceptor was constructed by insertional inactivation of the periplasmic and membrane-bound nitrate reductases. The mutant strain was able to grow aerobically with nitrate as the sole nitrogen source. It also grew anaerobically with nitrate as sole nitrogen source when nitrous oxide was provided as a respiratory electron acceptor. These growth characteristics are attributed to the presence of a third, assimilatory nitrate reductase. Nitrate reductase activity was detectable in intact cells and soluble fractions using nonphysiological electron donors. The enzyme activity was not detectable when ammonium was included in the growth medium. The results provide an unequivocal demonstration that P. denitrificans can express an assimilatory nitrate reductase in addition to the well-characterised periplasmic and membrane-bound nitrate reductases.
    Type of Medium: Electronic Resource
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  • 15
    Electronic Resource
    Electronic Resource
    Springer
    Antonie van Leeuwenhoek 66 (1994), S. 23-36 
    ISSN: 1572-9699
    Keywords: Denitrification ; FNR ; FNR homologues ; nitrogen fixation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Homologues of the transcriptional regulator FNR fromEscherichia coli have been identified in a variety of taxonomically diverse bacterial species. Despite being structurally very similar, members of the FNR family have disparate regulatory roles. Those fromShewanella putrefaciens, Pseudomonas aeruginosa, Pseudomonas stutzeri andRhodopseudomonas palustris are functionally similar to FNR in that they regulate anaerobic respiration or carbon metabolism. Four rhizobial proteins (fromRhizobium meliloti, R. leguminosarum, B. japonicum andAzorhizobium caulinodans) are involved in the regulation of nitrogen fixation; a fifth (fromRhizobium strain IC3342) has unknown function. Two proteins from mammalian pathogens (Actinobacillus pleuropneumoniae andBordetella pertussis) may be involved in the regulation of toxin expression. The FNR protein ofVibrio fischeri regulates bioluminescence, and the function of the one known FNR homologue from a Gram-positive organism (Lactobacillus casei) remains to be elucidated. Some members of this family, like FNR itself, appear to function as sensors of oxygen availability, whereas others do not. The ability to sense and respond to oxygen limitation may be correlated with the presence of cysteine residues which, in the case of FNR, are thought to be involved in oxygen or redox sensing. The mechanism of DNA sequence recognition is probably conserved, or very similar, throughout this family. In a number of other Gram-negative species, there is good indirect evidence for the existence of FNR analogues; these includeAlcaligenes eutrophus, A. denitrificans, A. faecalis, Paracoccus denitrificans and a number ofPseudomonas species.
    Type of Medium: Electronic Resource
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