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  • NADH oxidation  (2)
  • Springer  (2)
  • American Chemical Society (ACS)
  • 1
    Electronic Resource
    Electronic Resource
    Evidence for transmembrane electron transfer coupled to proton secretion in plasma membrane vesicles loaded by electroporation (1995)
    Springer
    Protoplasma 184 (1995), S. 22-30 
    Details
    ISSN: 1615-6102
    Keywords: NADH oxidation ; Plasma membrane ; Proton transport ; Redox chain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We demonstrate an in vitro trans plasma membrane electron transport from an encapsulated nucleotide to an external electron acceptor. Right-side-out vesicles prepared from soybean hypocotyls by aqueous two-phase partitioning were loaded with NADH by electroporation. Absence of calcium ions and an electric field strength of over 2 kV/cm was necessary for opening of the vesicles and importation of NADH. The presence of calcium ions was necessary for vesicle sealing. External NADH was removed with oxalacetate and malate dehydrogenase. If an impermeable electron acceptor was added to the exterior of the sealed vesicles, the oxidation of encapsulated NADH was increased, indicating a transmembrane electron transfer from an internal e− donor to the external e− acceptor analogous to that observed with intact cells. The ratio of NADH oxidized to hexacyanoferrat III reduced was 0.67. This indicates that NADH oxidation with oxygen as acceptor still occurred. Oxidation of the internal NADH was not affected by cyanide, azide, SOD or catalase but was inhibited by actinomycin D. Inhibition was also observed by the auxin 2,4-D, but by the inactive analog 2,3-D too. Oxidation of internal NADH both in absence and presence of the external acceptor, HCF III, showed a rapid decline in activity, which is relieved by the detergent Triton X-100, or the protonophore FCCP. Maximum NADH oxidation both with and without HCF III required an internal acidic pH gradient across the vesicle membrane. The results are consistent with a proton-gradient driving transplasma membrane NADH dehydrogenase which can transfer electrons to oxygen or an external impermeable oxidant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01276897
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  • 2
    Electronic Resource
    Electronic Resource
    A link between transport and plasma membrane redox system(s) in carrot cells (1984)
    Springer
    Journal of bioenergetics and biomembranes 16 (1984), S. 143-152 
    Details
    ISSN: 1573-6881
    Keywords: Plasma membrane ; NADH oxidation ; potassium transport ; ATPase inhibitors ; proton gradient generation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Carrot (Daucus carota L.) cells grown in suspension culture oxidized exogeneous NADH. The NADH oxidation was able to stimulate K+ (86Rb+) transport into cells, but it did not affect sucrose transport.N,N'-Dicyclohexyl-carbodiimide, diethylstilbestrol, and oligomycin, which only partially inhibited NADH oxidation, almost completely collapsed the K+ (86Rb+) transport. Vanadate, which is less effective as an ion transport inhibitor, was less effective in inhibiting the NADH-driven transport of K+ (86Rb+).p-Fluormethoxycarbonylcyanide phenylhydrazone inhibits the K+ transport over 90% including that induced by NADH. The results are interpreted as evidence that a plasma membrane redox system in root cells is closely associated with the ATPase which can drive K+ transport. Because of the inhibitor effects, it appears that membrane components common to the redox system and ATPase function in the transport of K+.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00743045
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