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  • Articles: DFG German National Licenses  (3)
  • 1995-1999  (2)
  • 1990-1994  (1)
  • seawater electrolysis  (2)
  • ATPase activity  (1)
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  • Articles: DFG German National Licenses  (3)
Material
Years
  • 1995-1999  (2)
  • 1990-1994  (1)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of applied electrochemistry 27 (1997), S. 1362-1368 
    ISSN: 1572-8838
    Keywords: manganese oxide electrode ; oxygen evolution ; seawater electrolysis ; surface activation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Electrical Engineering, Measurement and Control Technology
    Notes: Abstract Utilizing the fact that the equilibrium potential of oxygen evolution is lower than that of chlorine evolution, oxygen evolution in seawater electrolysis was enhanced by decreasing the polarization potential under galvanostatic conditions through increasing the effective surface area of manganese oxide electrodes. Electrodes were prepared by a thermal decomposition method. IrO2-coated titanium (IrO2/Ti electrode) was used as the substrate on which manganese oxide was coated (MnOX/IrO2/Ti electrode). Subsequently, oxide mixtures of manganese and zinc were coated (MnOX–ZnO/MnOX/IrO2/Ti electrode). The effective surface area of the MnOX–ZnO/MnOX/IrO2/Ti electrodes was increased by selective dissolution of zinc (leaching) into hot 6M KOH. The oxygen evolution efficiency of the MnOX/IrO2/Ti electrode was 68–70%. Leaching of zinc from the MnOX–ZnO/MnOX/IrO2/Ti electrodes with 25mol% or less zinc led to a significant increase in the oxygen evolution efficiency. The maximum efficiency attained was 86% after leaching of zinc from the MnOX–25mol%ZnO/MnOX/IrO2/Ti electrode. However, large amounts of zinc addition, such as 40mol% or more are detrimental because of a decrease in the oxygen evolution efficiency. This is due to the formation of a double oxide, ZnMnO3, which is hardly dissolved in hot 6M KOH.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1572-8838
    Keywords: anodic deposition ; manganese-molybdenum oxide electrode ; oxygen evolution ; seawater electrolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Electrical Engineering, Measurement and Control Technology
    Notes: Abstract Manganese-molybdenum oxide electrodes were prepared by anodic deposition on an IrO2-coated titanium substrate at a constant current density of 600Am−2 from baths containing 0.2M MnSO4 and 0–0.1M Na2MoO4 at 90∘C and pH 0.5. These electrodes were characterised for oxygen evolution in the electrolysis at 1,000Am−2 in 0.5M NaCl solution at 30∘C and pH 8 or 12. The most active and stable oxygen evolving anode exhibited 100% efficiency for oxygen evolution, and an efficiency of 98.5% for over 1,500 h at pH 12 and of 96.5% for over 2,800 h at pH 8 of continuous electrolysis. X-ray diffraction measurement and XPS analysis indicated that the deposits consist of a nanocrystalline single γ-MnO2 type phase, and manganese and molybdenum in the deposits are in the Mn4+ and Mo6+ states. The electrochemical studies showed that the manganese-molybdenum oxide electrodes drastically reduced the electrocatalytic activity for chlorine evolution to the undetectable level, resulting in 100% efficiency for oxygen evolution, although the addition of molybdenum slightly increased the oxygen overpotential.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 160 (1990), S. 233-239 
    ISSN: 1432-136X
    Keywords: Temperature ; Acclimation ; Myosin ; Myosin heavy chain ; ATPase activity ; Carp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Myosins were isolated from dorsal ordinary muscles of carp acclimated to 10°C and 30°C for a minimum of 5 weeks and examined for their ATPase activities. Ca2+-ATPase activity was different between myosins from cold-and warm-acclimated carp, especially at KCl concentrations ranging from 0.1 to 0.2 M, when measured at pH 7.0. The highest activity was 0.32 μmol Pi·min-1·mg-1 at 0.2 M KCl for cold-acclimated carp and 0.47 μmol Pi·min-1·mg-1 at 0.1 M KCl for warm-acclimated fish. The pH-dependency of Ca2+-ATPase activity at 0.5 M KCl for both carp was, however, similar exhibiting two maxima around 0.3 μmol Pi·min-1·mg-1 at pH 6 and 0.4 μmol Pi·min-1·mg-1 at pH 9. K+(EDTA)-ATPase activity at pH 7.0 neither exhibited differences between both myosins. It increased with increasing KCl concentration showing the highest value of about 0.4 μmol Pi·min-1·mg-1 at 0.6–0.7 M KCl. Actin-activated myosin Mg2+-ATPase activity was markedly different between cold-and warm-acclimated carp. The maximum initial velocity was 0.53 μmol Pi·min-1·mg-1 myosin at pH 7.0 and 0.05 M KCl for cold-acclimated carp, which was 1.6 times as high as that for warm-acclimated carp. These differences were in good agreement with those obtained with myofibrillar Mg2+-ATPase activity between both carp. No differences were, however, observed in myosin affinity to actin. Differences in myosin properties between cold- and warm-acclimated carp were further evidenced by its thermal stability. The inactivation rate constant of myosin Ca2+-ATPase was 25·10-4·s-1 at 30°C and pH 7.0 for cold-acclimated carp, which was about 4 times as high as that for warm-acclimated carp. Light chain composition did not differ between both carp myosins. The differences in a primary structure of the heavy chain subunit was, however, clearly demonstrated between both myosins by peptide mapping.
    Type of Medium: Electronic Resource
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