ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Cytochromec oxidase metal centers: Location and function (1991)
    Springer
    Journal of bioenergetics and biomembranes 23 (1991), S. 291-302 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00762223
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...