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  • 1
    Electronic Resource
    Electronic Resource
    Occurrence of xanthine dehydrogenase in Chlamydomonas reinhardii: A common cofactor shared by xanthine dehydrogenase and nitrate reductase (1981)
    Springer
    Planta 153 (1981), S. 254-257 
    Details
    ISSN: 1432-2048
    Keywords: Chlamydomonas (mutants) ; Nitrate reductase ; Xanthine dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Wild-type Chlamydomonas reinhardii cells have xanthine dehydrogenase activity when grown with nitrate, nitrite, urea, or amino acid media. Mutant strains 102, 104, and 307 of Chlamydomonas, lacking both xanthine dehydrogenase and nitrate reductase activities, were incapable of restoring the NADPH-nitrate reductase activity of the mutant nit-1 of Neurospora crassa, whereas wild type cells and mutants 203 and 305 had xanthine dehydrogenase and were able to reconstitute the nitrate reductase activity of nit-1 of Neurospora. Therefore, it is concluded that in Chlamydomonas a common cofactor is shared by xanthine dehydrogenase and nitrate reductase. Xanthine dehydrogenase is repressed by ammonia and seems to be inessential for growth of Chlamydomonas.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00383895
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  • 2
    Electronic Resource
    Electronic Resource
    Assimilatory nitrate reductase from Acinetobacter calcoaceticus (1977)
    Springer
    Archives of microbiology 112 (1977), S. 127-132 
    Details
    ISSN: 1432-072X
    Keywords: Acinetobacter calcoaceticus ; Nitrate reductase ; Interconversion ; Cyanate ; Enzyme synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A soluble nitrate reductase from the bacterium Acinetobacter calcoaceticus grown on nitrate has been characterized. The reduction of nitrate to nitrite is mediated by an enzyme of 96000 molecular weight that can use as electron donors either viologen dyes chemically reduced with dithionite or enzymatically reduced with NAD(P)H, through specific diaphorases which utilize viologens as electron acceptors. Nitrate reductase activity is molybdenum-dependent as shown by tungstate antagonistic experiments and is sensitive to -SH reagents and metal chelators such as KCN. The enzyme synthesis is repressed by ammonia. Moreover, nitrate reductase activity undergoes a quick inactivation either by dithionite and temperature or by dithionite in the presence of small amounts of nitrate. Cyanate prevents this inactivating process and can restore the activity once the inactivation had occurred, thus suggesting that an interconversion mechanism may participate in the regulation of Acinetobacter nitrate reductase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00429324
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