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  • 1
    Electronic Resource
    Electronic Resource
    Plasmid pMOL28-mediated inducible nickel resistance in Alcaligenes eutrophus strain CH34 (1987)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 43 (1987), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The effect of nickel salt on growth of the nickel-resistant wild type strain Alcaligenes eutrophus CH34, which harbours two plasmids, and on its partially or totally cured derivatives as well as of the wild type strain H16 was studied. Plasmid pMOL28-mediated nickel resistance turned out to be an inducible property. Full resistance is induced during growth in the presence of 0.03–3.0 mM NiCl2. Induction requires growth. While plasmid-free cells accumulate nickel at a high rate, the pMOL28-harbouring-induced cells accumulate only negligibly small amounts of nickel. It is concluded that pMOL28 mediates a protective mechanism preventing the cells to accumulate nickel ions intracellularly at toxic concentrations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02089.x
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  • 2
    Electronic Resource
    Electronic Resource
    Nickel resistance of Alcaligenes denitrificans strain 4a-2 is chromosomally coded (1990)
    Springer
    Archives of microbiology 154 (1990), S. 133-138 
    Details
    ISSN: 1432-072X
    Keywords: Alcaligenes denitrificans ; Alcaligenes eutrophus ; Nickel resistance ; Hydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A newly isolated aerobic hydrogen-oxidizing bacterium, Alcaligenes denitrificans strain 4a-2, differs from related autotrophic bacteria by containing only a single cytoplasmic, NAD-reducing hydrogenase, and by its high resistance to nickel ions, i.e. tolerance to 20 mM NiCl2. Strain 4a-2 harbors a single plasmid of about 250 kb. On helper-assisted mating of 4a-2 with Alcaligenes eutrophus strains H16,G29, and M85 nickelresistant transconjugants were selected; these did not contain the donor plasmid, however. All three transconjugants tolerated 3 to 10 mM NiCl2. The resistance was constitutively expressed. DNA/DNA hybridization showed homology with EcoRI-digested DNA of the wild type 4a-2 and transconjugants using a DNA probe containing nickel resistance genes of pMOL28. This indicated that the 4a-2 nickel resistance genes are located on the chromosome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00423322
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of the membranous denitrification enzymes nitrite reductase (cytochrome cd1) and copper-containing nitrous oxide reductase from Thiobacillus denitrificans (1996)
    Springer
    Archives of microbiology 165 (1996), S. 55-61 
    Details
    ISSN: 1432-072X
    Keywords: Key words Cytochrome cd1 ; Nitrite reductase ; Nitrous ; oxide reductase ; Denitrification ; Thiobacillus ; denitrificans ; Pseudomonas stutzeri ; DNA hybridization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cytochrome cd 1-nitrite reductase and nitrous oxide reductase of Thiobacillus denitrificans were purified and characterized by biochemical and immunochemical methods. In contrast to the generally soluble nature of the denitrification enzymes, these two enzymes were isolated from the membrane fraction of T. denitrificans and remained active after solubilization with Triton X-100. The properties of the membrane-derived enzymes were similar to those of their soluble counterparts from the same organism. Nitrous oxide reductase activity was inhibited by acetylene. Nitrite reductase and nitrous oxide reductase cross-reacted with antisera raised against the soluble enzymes from Pseudomonas stutzeri. The nirS, norBC, and nosZ genes encoding the cytochrome cd 1-nitrite reductase, nitric oxide reductase, and nitrous oxide reductase, respectively, from P. stutzeri hybridized with genomic DNA from T. denitrificans. Cross-reactivity and similar N-terminal amino acid and gene sequences suggest that the primary structures of the Thiobacillus enzymes are homologous to the soluble proteins from P. stutzeri.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050296
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  • 4
    Electronic Resource
    Electronic Resource
    The Alcaligenes eutrophus hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase, is required for heme biosynthesis during anaerobic growth (1997)
    Springer
    Archives of microbiology 169 (1997), S. 52-60 
    Details
    ISSN: 1432-072X
    Keywords: Key wordshemN ; Denitrification ; Anaerobic heme biosynthesis ; Alcaligenes eutrophus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The insertion mutant HF231 of Alcaligenes eutrophus H16 failed to grow anaerobically on nitrate and nitrite. When grown under oxygen limitation, mutant HF231 specifically excreted coproporphyrin III, an intermediate of heme biosynthesis. With the help of a Tn5-labeled fragment, we identified and cloned the corresponding wild-type fragment. Sequence analysis of the mutant locus revealed an open reading frame consisting of 1,473 bp, predicting a protein of 491 amino acids that corresponds to a size of 54.2 kDa. In the non-coding upstream region, consensus elements that are indicative for binding sites of the anaerobic transcriptional regulator Fnr were identified. The deduced polypeptide showed extensive sequence similarity with various bacterial oxygen-independent coproporphyrinogen III oxidases designated HemN. HemN catalyzes the oxidative decarboxylation of coproporphyrinogen III to yield protoporphyrinogen IX. Anaerobic growth on nitrate and nitrite of mutant HF231 was restored by introducing the hemN gene of A. eutrophus or of Pseudomonas aeruginosa on a broad-host-range vector. Likewise, the A. eutrophus hemN complemented heme biosynthesis of a Salmonella typhimurium hemF/hemN double mutant during anaerobic and aerobic growth. Analysis of a transcriptional lacZ gene fusion showed that expression of hemN in A. eutrophus is nitrate-independent and repressed by oxygen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050540
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  • 5
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray diffraction studies of a bacterial flavohemoglobin protein (1995)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 21 (1995), S. 351-353 
    Details
    ISSN: 0887-3585
    Keywords: protein crystallization ; X-ray crystallography ; flavoprotein ; hemoglobin ; electron transfer ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A flavohemoglobin protein (FHP) was isolated from Alcaligenes eutrophus and has been crystallized by vapor diffusion methods using PEG 3350 as precipitant. The crystals of the FAD- and heme-containing protein belong to the monoclinic space group P21 with unit cell parameters of 52.2 Å, 85.8 Å, 103.9 Å, and 81.8° corresponding to two molecules per asymmetric unit. The crystals diffract at least to a resolution of 2.0 Å and are suitable for an X-ray structure analysis. © 1995 Wiley-Liss, Inc.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340210408
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