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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 148 (1987), S. 52-56 
    ISSN: 1432-072X
    Keywords: Methanogenic bacteria ; Sulfate-reducing bacteria ; Acetogenic bacteria ; Corrinoid ; Methane formation ; Cobalt ; Membrane cobamide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In Methanobacterium thermoautotrophicum a corrinoid-carrying membrane protein complex has been found, to which a tentative role in methane formation has been ascribed. To test this hypothesis representatives from different orders of methanogenic bacteria were examined for membrane-bound cobamides. These species differed in cell carbon precursor, in methane precursor, in occurrence of cytochromes and of the enzyme CO dehydrogenase, and in the systematic position (Methanobacteriales, Methanomicrobiales). All methanogenic bacteria contained cobamides in the membranes in amounts of about 60 nmol/g cell dry weight, in addition to different amounts of cobamides in the soluble cell fraction. The only central metabolic reaction obviously common to all of these methanogens was methyl coenzyme M reduction to CH4. It is concluded that the membrane corrinoid participates in this energy-conserving reaction. Sulfate-reducing and acetogenic bacteria were included in this survey. They contained different amounts of cobamides in the soluble cell fraction but not in the membrane, a possible exception being Acetobacterium woodii.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 152 (1989), S. 273-279 
    ISSN: 1432-072X
    Keywords: Alicyclic compounds ; Denitrification ; Cyclohexanol dehydrogenase ; Cyclohexanone dehydrogenase ; 2-Cyclohexenone hydratase ; 3-Hydroxycyclohexanone dehydrogenase ; 1,3-Cyclohexanedione hydrolase ; Phenol ; Aromatization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The enzymes involved in the anaerobic degration of cyclohexanol were searched for in a denitrifying Pseudomonas species which metabolizes this alicyclic compound to CO2 anaerobically. All postulated enzyme activities were demonstrated in vitro with sufficient specific activities. Cyclohexanol dehydrogenase catalyzes the oxidation of the substrate to cyclohexanone. Cyclohexanone dehydrogenase oxidizes cyclohexanone to 2-cyclohexenone. 2-Cyclohexenone hydratase and 3-hydroxycyclohexanone dehydrogenase convert 2-cyclohexenone via 3-hydroxycyclohexanone into 1,3-cyclohexanedione. Finally, the dione is cleaved by 1,3-cyclohexanedione hydrolase into 5-oxocaproic acid. Some kinetic and regulatory properties of these enzymes were studied.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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