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  • 1
    Electronic Resource
    Electronic Resource
    Anaerobic ammonia oxidation with nitrogen dioxide by Nitrosomonas eutropha (1997)
    Springer
    Archives of microbiology 167 (1997), S. 106-111 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsNitrosomonas ; Anaerobic ammonia ; oxidation ; Anaerobic cell growth ; Nitrogen dioxide ; Nitric oxide ; Nitrous oxide ; Dinitrogen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Nitrosomonas eutropha, an obligately lithoautotrophic bacterium, was able to nitrify and denitrify simultaneously under anoxic conditions when gaseous nitrogen dioxide (NO2) was supplemented to the atmosphere. In the presence of gaseous NO2, ammonia was oxidized, nitrite and nitric oxide (NO) were formed, and hydroxylamine occurred as an intermediate. Between 40 and 60% of the produced nitrite was denitrified to dinitrogen (N2). Nitrous oxide (N2O) was shown to be an intermediate of denitrification. Under an N2 atmosphere supplemented with 25 ppm NO2 and 300 ppm CO2, the amount of cell protein increased by 0.87 mg protein per mmol ammonia oxidized, and the cell number of N. eutropha increased by 5.8 × 109 cells per mmol ammonia oxidized. In addition, the ATP and NADH content increased by 4.3 μmol ATP (g protein)–1 and 6.3 μmol NADH (g protein)–1 and was about the same in both anaerobically and aerobically grown cells. Without NO2, the ATP content decreased by 0.7 μmol (g protein)–1, and the NADH content decreased by 1.2 μmol (g protein)–1. NO was shown to inhibit anaerobic ammonia oxidation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050422
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  • 2
    Electronic Resource
    Electronic Resource
    Prevention of lens protein glycation by taurine (1997)
    Springer
    Molecular and cellular biochemistry 177 (1997), S. 245-250 
    Details
    ISSN: 1573-4919
    Keywords: cataract ; crystalline ; glycation ; oxidation ; taurine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Modifications in lens protein structure and function due to nonenzymic glycosylation and oxidation have been suggested to play a significant role in the pathogenesis of sugar and senile cataracts. The glycation reaction involves an initial Schiff base formation between the protein NH2 groups and the carbonyl group of a reducing sugar. The Schiff base then undergoes several structural modifications, via some oxidative reactions involving oxygen free radicals. Hence certain endogenous tissue components that may inhibit the formation of protein-sugar adduct formation may have a sparing effect against the cataractogenic effects of sugars and reactive oxygen. The eye lens is endowed with significant concentration of taurine, a sulfonated amino acid, and its precursor hypotaurine. It is hypothesized that taurine and hypotaurine may have this purported function of protecting the lens proteins against glycation and subsequent denaturation, in addition to their other functions. The results presented herein suggest that these compounds are indeed capable of protecting glycation competitively by forming Schiff bases with sugar carbonyls, and thereby preventing the glycation of lens proteins per se. In addition, they appear to prevent oxidative damage by scavenging hydroxyl radicals. This was apparent by their preventive effect against the formation of the thiobarbituric acid reactive material generated from deoxy-ribose, when the later was exposed to hydroxyl radicals generated by the action of xanthine oxidase on hypoxanthine in presence of iron.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006863322454
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  • 3
    Electronic Resource
    Electronic Resource
    An Uncoupling of the Processes of Oxidation and Phosphorylation in Glycolysis (1997)
    Springer
    Bioscience reports 17 (1997), S. 521-527 
    Details
    ISSN: 1573-4935
    Keywords: Glyceraldehyde-3-phosphate dehydrogenase ; glycolysis ; oxidation ; uncoupling ; thiols ; hydrogen peroxide ; mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Data on alterations of the properties of glyceraldehyde-3-phosphate dehydrogenase upon oxidation of its functional groups are reviewed; a mechanism of uncoupling of oxidation and phosphorylation in glycolysis is considered. Possible ways of regulating uncoupling, and the physiological importance of this process, are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1027356106330
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