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  • 1
    Electronic Resource
    Electronic Resource
    Close genetic relationship between Nitrobacter hamburgensis nitrite oxidoreductase and Escherichia coli nitrate reductases (1993)
    Springer
    Archives of microbiology 160 (1993), S. 447-453 
    Details
    ISSN: 1432-072X
    Keywords: Nitrobacter hamburgensis ; Nitrite oxidore-ductase genes ; Nitrite oxidoreductase β-subunit ; Ironsulfur protein ; Escherichia coli nitrate reductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nitrite oxidoreductase (NOR) from the facultative nitrite-oxidizing bacterium Nitrobacter hamburgensis X14 was investigated genetically. In order to develop a probe for the gene norB, the N-terminal amino acid sequence of the NOR β-subunit (NorB) was determined. Based on that amino acid sequence, an oligo-nucleotide was derived that was used for the identification and cloning of gene norB. Sequence analysis of DNA fragments revealed three adjacent open reading frames in the order norA, norX, norB. The DNA sequences of norX and norB represented complete genes while the open reading frame of norA was truncated by the cloning site. The deduced amino acid sequence of protein NorB contained four cysteine clusters with striking homology to those of iron-sulfur centers of bacterial ferredoxins. NorB shares significant sequence similarity to the β-subunits (NarH, NarY) of the two dissimilatory nitrate reductases (NRA, NRZ) of Escherichia coli. Additionally, the derived amino acid sequence of the truncated open reading frame of norA showed striking resemblance to the α-subunits (NarG, NarZ) of the E. coli nitrate reductases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245305
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Membrane-bound nitrite oxidoreductase of Nitrobacter: evidence for a nitrate reductase system (1984)
    Springer
    Archives of microbiology 140 (1984), S. 153-158 
    Details
    ISSN: 1432-072X
    Keywords: Nitrobacter hamburgensis ; Nitrite oxidoreductase ; Nitrate reductase ; Molybdenum iron-sulfur protein ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Nitrite oxidoreductase, the essential enzyme complex of nitrite oxidizing membranes, was isolated from cells of the nitrifying bacterium Nitrobacter hamburgensis. The enzyme system was solubilized and purified in the presence of 0.25% sodium deoxycholate. Nitrite oxidoreductase oxidized nitrite to nitrate in the presence of ferricyanide. The pH optimum was 8.0, and the apparent K m value for nitrite amounted to 3.6 mM. With reduced methyl-and benzylviologen nitrite oxidoreductase exhibited nitrate reductase activity with an apparent K m value of 0.9 mM for nitrate. NADH was also a suitable electron donor for nitrate reduction. The pH optimum was 7.0. Treatment with SDS resulted in the dissociation into 3 subunits of 116,000, 65,000 and 32,000. The enzyme complex contained iron, molydbenum, sulfur and copper. A c-type cytochrome was present. Isolated nitrite oxidoreductase is a particle of 95±30 Å in diameter.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00454918
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Association of acid-producing thiobacilli with degradation of concrete: analysis by ‘signature’ fatty acids from the polar lipids and lipopolysaccharide (1987)
    Springer
    Journal of industrial microbiology and biotechnology 2 (1987), S. 63-69 
    Details
    ISSN: 1476-5535
    Keywords: Concrete biodegradation ; Signature lipid ; Fatty acid ; Thiobacilli ; Acid-producing bacteria ; Hydroxy-cyclopropyl fatty acid ; Methoxy fatty acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The acid-producing thiobacilli contain fatty acid components in the polar lipids and lipopolysaccharide lipid A that are sufficiently unusual that they can be utilized as ‘signature’ lipid biomarkers for these organisms in environmental samples. Studies in microcosms have shown correlations between activity of these organisms, measured by recovery and viable counting, and the degradation of concrete. The ‘signature’ lipid analysis provides a detection assay requiring neither separation of the organisms from the substratum nor growth prior to determination. The presence of acid-producing thiobacilli was demonstrated in microcosm samples and degenerating concrete from the Hamburg (F.R.G.) sewer system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01569504
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    Paper (German National Licenses)
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