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  • 1
    Electronic Resource
    Electronic Resource
    Studies on the molecular basis of H+ translocation by cytochromec oxidase (1981)
    Springer
    Journal of bioenergetics and biomembranes 13 (1981), S. 219-228 
    Details
    ISSN: 1573-6881
    Keywords: cytochrome ; oxidase ; mitochondria ; structure membrane ; protein ; subunits ; oxidation-reduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract We report here studies which characterize further the interaction ofN,N′-dicyclohexylcarbodiimide with cytochromec oxidase leading to inhibition of H+ translocation by the enzyme. Further evidence is presented to show that the inhibition results from a real interaction of DCCD with the enzyme and cannot be accounted for by uncoupling and, contrary to recent criticisms, this interaction occurs specifically with subunit III of the enzyme even at relatively high inhibitor-to-enzyme stoichiometries. Use of a spin-label analogue of DCCD has enabled us to demonstrate that the carbodiimide-binding site is highly apolar and may not lie on the pathway of electron transfer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00743201
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  • 2
    Electronic Resource
    Electronic Resource
    Morphology of proteoliposomes containing fluorescein-phosphatidylethanolamine reconstituted with native and subunit III-depleted cytochromec oxidase (1985)
    Springer
    Journal of bioenergetics and biomembranes 17 (1985), S. 385-393 
    Details
    ISSN: 1573-6881
    Keywords: Cytochromec oxidase ; fluorescein-phosphatidylethanolamine ; proteoliposomes ; rapid freezing ; freeze-fracture size analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Beef heart cytochromec oxidase was reconstituted in asolectin liposomes containing the pH indicator fluorescein-phosphatidylethanolamine (FPE) by the cholate-dialysis procedure. The influence of PFE on the asolectin liposome size and of the removal of subunit III from the complex on its incorporation into liposomes was analyzed by freeze-fracture electron microscopy. Samples were frozen without the addition of cryoprotectants. The vesicle size distribution of native enzyme reconstituted into asolectin liposomes was homogenous, 84% of the population having a diameter of 14–37 ± 7.5 mm. The preparation containing FPE had a similar vesicle size distribution, but with bigger diameter range (20–50 nm). In all three different types of proteoliposome preparations the majority of particles containing vesicles was found to have 1 particle (42–81%). The absence of subunit III did not influence the incorporation of the enzyme into the liposomes and was as good as the preparation with native enzyme (〉99%). Therefore we conclude that the suppression of the proton pump activity was due to the intrinsic properties of subunit III and not to defective incorporation into artificial membrane systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00743111
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