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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 27 (1988), S. 7546-7551 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 386 (1997), S. 320-320 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Sir - I read with interest the News story about the issues raised by Japan's demography, showing that a dramatic increase in population age is being accompanied by a decrease in the number of financially productive individuals (Nature 385,379; 1997). The extrapolations that can be made from ...
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 147 (1969), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 147 (1969), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 358 (1980), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 13 (1981), S. 219-228 
    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.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 18 (1986), S. 277-284 
    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].
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 8 (1976), S. 257-269 
    ISSN: 1573-6881
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Conclusions It is possible to conclude, after the discussion on the application of different probes to energy-transducing membranes, that the efforts in the direction of the elucidation of the mechanism of energy conservation have not been wasted. Despite the lack of a final answer to the question whether the coupling device is chemiosmotic, chemical, or conformational in nature, a number of new important experiments have been performed which will finally contribute to the solution of the problem. Apart from the important characterization of a number of physical parameters regarding the phospholipid environment and the interaction among proteins in the membrane, data concerning the onset of membrane potential(s) and pH gradients associated with energy conservation appear convincing. In fact, from different types of approach (lipophylic ions, charged fluorescent probes, carotenoids, and merocyanines) a common conclusion can be reached, namely that electrical potentials are set at the level of the mitochondrial and other energy-transducing membranes. There is still some controversy as to whether the potential is set across the entire thickness or only a small portion of the membrane. It appears also well established that pH gradients are set across the coupling membrane during energy conservation and that pH gradients and membrane potentials have specific correlations. Whether the conclusions reached with the probe technique are perfectly in line with the chemiosmotic hypothesis, require some modification of it, or may also fit with a chemical hypothesis would go beyond the purpose of the present discussion. It seems, however, that some predictions of the chemiosmotic hypothesis have been, at least qualitatively, confirmed by the use of the probe approach described above.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 17 (1985), S. 385-393 
    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
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 23 (1991), S. 291-302 
    ISSN: 1573-6881
    Keywords: Paracoccus denitrificans ; Cytochromec oxidase ; hemea ; copper A, B, and C ; electron transfer ; proton pump
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Cytochromec oxidase ofParacoccus denitrificans is spectroscopically and functionally very similar to the mammalian enzyme. However, it has a very much simpler quaternary structure, consisting of only three subunits instead of the 13 of the bovine enzyme. The known primary structure of theParacoccus denitrificans subunits, the knowledge of a large number of sequences from other species, and data on the controlled proteolytic digestion of the enzyme allow structural restrictions to be placed on the models describing the binding of the active metal centers to the polypeptide structure.
    Type of Medium: Electronic Resource
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