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  • ruthenium  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Electron transfer from cytochromeb 5 to cytochromec (1995)
    Springer
    Journal of bioenergetics and biomembranes 27 (1995), S. 331-340 
    Details
    ISSN: 1573-6881
    Keywords: Cytochromeb 5 ; cytochromec ; electron transfer ; kinetics ; ruthenium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The reaction of cytochromeb 5 with cytochromec has become a very prominent system for investigating fundamental questions regarding interprotein electron transfer. One of the first computer modeling studies of electron transfer and protein/protein interaction was reported using this system. Subsequently, numerous studies focused on the experimental determination of the features which control protein/protein interactions. Kinetic measurements of the intracomplex electron transfer reaction have only appeared in the last 10 years. The current review will provide a summary of the kinetic measurements and a critical assessment of the interpretation of these experiments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02110102
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Electron transfer between cytochromec and cytochromec peroxidase (1995)
    Springer
    Journal of bioenergetics and biomembranes 27 (1995), S. 341-351 
    Details
    ISSN: 1573-6881
    Keywords: Electron transfer ; cytochromec ; cytochromec peroxidase ; ruthenium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The reaction between cytochromec (CC) and cytochromec peroxidase (CcP) is a very attractive system for investigating the fundamental mechanism of biological electron transfer. The resting ferric state of CcP is oxidized by hydrogen peroxide to compound I (CMPI) containing an oxyferryl heme and an indolyl radical cation on Trp-191. CMPI is sequentially reduced to CMPII and then to the resting state CcP by two molecules of CC. In this review we discuss the use of a new ruthenium photoreduction technique and other rapid kinetic techniques to address the following important questions: (1) What is the initial electron acceptor in CMPI? (2) What are the true rates of electron transfer from CC to the radical cation and to the oxyferryl heme? (3) What are the binding domains and pathways for electron transfer from CC to the radical cation and the oxyferryl heme? (4) What is the mechanism for the complete reaction under physiological conditions?
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02110103
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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