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  • 1
    Electronic Resource
    Electronic Resource
    Further Characterization of Nitrate and Nitrite Reductases from Chlamydomonas reinhardii (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 36 (1976), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The enzymes responsible for nitrate reduction in Chlamydomonas reinhardii, namely NADH-nitrate reductase and ferredoxin-nitrite reductase, have been further characterized. The first activity of the nitrate reducing complex, NADH-diaphorase, is protected by FAD against thermic inactivation. This fact suggests an important structural and functional role for this nucleotide in the first moiety of the nitrate reductase complex. The effect of p-hydroxymercuribenzoate on the diaphorase activity and the protection by NADH against its inactivation indicate that some—SH groups participate in the electron transfer mediated by diaphorase.Radioactive labelling of nitrate reductase with 99Mo and 185W as well as competition experiments between Mo and W indicate that molybdenum is an essential component of terminal nitrate reductase activity. Iron seems to participate in the redox processes mediated by both nitrate and nitrite reductases as suggested by experiments performed at physiological level. Finally a tentative mechanism for the whole process of nitrate assimilation in Chlamydomonas is proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1976.tb02251.x
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  • 2
    Electronic Resource
    Electronic Resource
    Assimilatory nitrite-reductase from Rhodopseudomonas capsulata E1F1 (1981)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 11 (1981), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1981.tb06974.x
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  • 3
    Electronic Resource
    Electronic Resource
    Ammonia assimilation pathways in Rhodopseudomonas capsulata E1F1 (1983)
    Springer
    Archives of microbiology 136 (1983), S. 147-151 
    Details
    ISSN: 1432-072X
    Keywords: Ammonia assimilation ; l-Alanine dehydrogenase ; l-Alanine: 2-oxoglutarate aminotransferase ; R. capsulata E1F1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Rhodopseudomonas capsulata E1F1 growing phototrophically in different inorganic nitrogen sources assimilated ammonia through the reactions of the glutamine synthetase/glutamate synthase (GS/GOGAT) pathway. Addition of either methionine sulphoximine (MSX) or azaserine to N2-fixing cells resulted in the cessation of growth, which did not occur when these inhibitors were added to bacteria growing on l-glutamate. In nitrate-assimilating cells MSX or azaserine prevented both growth and nitrate uptake with simultaneous excretion of ammonia to the medium. In addition, MSX inactivated glutamine synthetase but neither glutamate synthase nor nitrate reductase, which, in contrast, were inactivated by azaserine. The excreted ammonia was taken up together with nitrate once growth was resumed, this uptake being coincident with the appearance of an NADPH-linked alanine dehydrogenase aminating activity and a marked increase of alanine: 2-oxoglutarate aminotransferase levels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00404790
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  • 4
    Electronic Resource
    Electronic Resource
    The nitrate-reducing enzyme system of Chlamydomonas reinhardii (1975)
    Springer
    Archives of microbiology 105 (1975), S. 21-25 
    Details
    ISSN: 1432-072X
    Keywords: Chlamydomonas reinhardii ; Nitrate Reductase ; Nitrite Reductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In Chlamydomonas reinhardii the reduction of nitrate to ammonia occurs in two independent enzymatic steps: 1. the two-electrons reduction of nitrate to nitrite catalyzed by NADH-nitrate reductase, and, 2. the six-electrons reduction of nitrite to ammonia catalyzed by ferredoxin-nitrite reductase. Both enzymes have been purified and characterized, and some of their properties have been studied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00447107
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  • 5
    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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  • 6
    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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  • 7
    Electronic Resource
    Electronic Resource
    The inorganic biochemistry of nitrogen bioenergetic processes (1979)
    Springer
    Naturwissenschaften 66 (1979), S. 81-88 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Notes: Abstract Redox conversions of inorganic nitrogen compounds are used by nitrate respiring, denitrifying and nitrifying bacteria to drive electron-transport phosphorylation. A preliminary understanding of these processes with respect to participating components and reaction sequences has now emerged. In particular, recent work suggests an involvement of membrane phenomena of chemiosmotic origin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00373498
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  • 8
    Electronic Resource
    Electronic Resource
    Nitrate reduction by photosynthetic purple bacteria (1982)
    Springer
    Photosynthesis research 3 (1982), S. 3-18 
    Details
    ISSN: 1573-5079
    Keywords: nitrate reduction ; purple bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00030045
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  • 9
    Electronic Resource
    Electronic Resource
    Effect of light and darkness on nitrate assimilation by Rhodopseudomonas capsulata E1F1 (1982)
    Springer
    Photosynthesis research 3 (1982), S. 313-319 
    Details
    ISSN: 1573-5079
    Keywords: aerobiosis ; anaerobiosis ; dark light ; nitrate assimilation ; phototrophic bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The photosynthetic nonsulfur purple bacterium Rhodopseudomonas capsulata strain E1F1 assimilated nitrate or nitrite only in illuminated cultures under anaerobic conditions. The bacterial cells grew aerobically in the dark only when ammonia or other forms of reduced nitrogen were present in the medium. However, nitrate reductase was detected either in light-anaerobic or in dark-aerobic conditions upon addition of nitrate to the media. Changes from light-anaerobic to dark-aerobic conditions and vice versa markedly influenced growth, nitrate uptake and the nitrate reductase levels. Growth on nitrate in the light and nitrate reductase activity were dependent on the presence of molybdenum in the medium whereas the addition of tungstate inhibited both growth and enzyme activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00034112
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  • 10
    Electronic Resource
    Electronic Resource
    High-conversion polymerization. I. Theory and application to methyl methacrylate (1976)
    New York : Wiley-Blackwell
    Journal of Polymer Science: Polymer Chemistry Edition 14 (1976), S. 883-897 
    Details
    ISSN: 0360-6376
    Keywords: Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The concept of polymer entanglements has been applied in conjunction with classical free-radical kinetics to describe vinyl polymerizations carried to high conversion. A kinetic model has been developed on the assumption that two populations of radicals exist in a high-conversion polymerization system: those radicals whose chain lengths are long enough to become entangled with neighboring molecules and have, therefore, a restricted mobility; and those shorter radicals whose mobilities are not strongly affected by diffusional effects. It has also been assumed that the kinetic rate constant for the termination step between entangled radicals is inversely proportional to the mean entanglement density. The model contains only two parameters in addition to the kinetic rate constants required to describe low-conversion polymerizations. One of these parameters can be determined, at least in principle, from measurements of solution properties of the polymer-monomer mixtures. The model so developed has been tested against experimental data obtained from the literature on the bulk polymerization of methyl methacrylate. The agreement between predicted and experimental monomer conversions and molecular weight averages is found to be satisfactory.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pol.1976.170140409
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