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  • 1
    Electronic Resource
    Electronic Resource
    Isolation of an anaerobic bacterium which reductively dechlorinates tetrachloroethene and trichloroethene (1996)
    Springer
    Biodegradation 7 (1996), S. 507-511 
    Details
    ISSN: 1572-9729
    Keywords: anaerobic respiration ; Dehalobacter restrictus ; reductive dehalogenation ; 16S rRNA sequence ; tetrachloroethene ; trichloroethene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Energy, Environment Protection, Nuclear Power Engineering , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Strain TEA, a strictly anaerobic, motile rod with one to four lateral flagella and a crystalline surface layer was isolated from a mixed culture that completely reduces chlorinated ethenes to ethene. The organism coupled reductive dehalogenation of tetrachloroethene or trichloroethene to cis-1,2-dichloroethene to growth, using molecular hydrogen as the electron donor. It was unable to grow fermentatively or in the presence of tri- or tetrachloroethene with glucose, pyruvate, lactate, acetate or formate. The 16S rDNA sequence of strain TEA was 99.7% identical to that of Dehalobacter restrictus. The two organisms thus are representatives of the same species or the same genus within the Bacillus/Clostridium subphylum of the gram-positive bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00115297
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  • 2
    Electronic Resource
    Electronic Resource
    The malonate decarboxylase enzyme system of Malonomonas rubra: evidence for the cytoplasmic location of the biotin-containing component (1993)
    Springer
    Archives of microbiology 160 (1993), S. 126-131 
    Details
    ISSN: 1432-072X
    Keywords: Malonomonas rubra ; Propionigenium modestum ; Malonate decarboxylase ; Methylmalonyl-CoA decarboxylase ; Biotin ; Avidin ; Electron microscopy ; High pressure freezing ; Immunolabeling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Malonate decarboxylase of Malonomonas rubra is a complex enzyme system involving cytoplasmic and membrane-bound components. One of these is a biotin-containing protein of Mr 120'000, the location of which in the cytoplasm was deduced from the following criteria: (i) If the cytoplasm was incubated with avidin and the malonate decarboxylase subsequently completed with the membrane fraction the decarboxylase activity was abolished. The corresponding incubation of the membrane with avidin, however, was without effect. (ii) Western blot analysis identified the single biotin-containing polypeptide of Mr 120'000 within the cytoplasm. (iii) Transmission electron micrographs of immuno-gold labeled M. rubra cells clearly showed the location of the biotinyl protein within the cytoplasm, whereas the same procedure with Propionigenium modestum cells indicated the location of the biotin enzyme methylmalonyl-CoA decarboxylase in the cell membrane. The biotin-containing protein of the M. rubra malonate decarboxylase enzyme system was not retained by monomeric avidin-Sepharose columns but could be isolated with this column in a catalytically inactive form in the presence of detergents. If the high binding affinity of tetrameric avidin towards biotin was reduced by destructing part of the tryptophan residues by irradiation or oxidation with periodate, the inhibition of malonate decarboxylase by the modified avidin was partially reversed with an excess of biotin. Attempts to purify the biotin protein in its catalytically active state using modified avidin columns were without success.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00288714
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