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  • 1
    Electronic Resource
    Electronic Resource
    Cytochromec oxidase fromParacoccus denitrificans in Triton X-100: Aggregation state and kinetics (1986)
    Springer
    Journal of bioenergetics and biomembranes 18 (1986), S. 277-284 
    Details
    ISSN: 1573-6881
    Keywords: Cytochromec oxidase ; aggregation state ; steady-state kinetics ; Paracoccus denitrificans ; molecular weight
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Cytochromec oxidase fromParacoccus denitrificans was homogenously dispersed in Triton X-100. Using gel exclusion chromatography and sucrose gradient centrifugation analysis a molecular weight of the detergent-protein complex of 155,000 was determined. After subtraction of the bound detergent (111 mol/mol hemeaa 3) a molecular weight of 85,000 resulted, which agreed well with the model of a monomer containing two subunits. This monomer showed high cytochromec oxidase activity when measured spectrophotometrically in the presence of Triton X-100 (V max=85 s−1). The molecular activity, plotted according to Eadie-Hofstee, was monophasic as a function of the cytochromec concentration. AK m of 3.6×10−6 M was evaluated, similar to theK m observed in the presence of dodecyl maltoside [Nałeczet al. (1985).Biochim. Biophys. Acta 808, 259–272].
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00743048
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  • 2
    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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