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    Kinetics and mechanism of the reduction of ferricytochrome c by the superoxide anion.

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    Authors
    Butler, John
    Koppenol, W H
    Margoliash, E
    Affiliation
    Department of Biophysical Chemistry, Paterson Laboratories, Christie Hospital and Holt Radium Institute, Manchester, M20 9BX, United Kingdom
    Issue Date
    1982-09-25
    
    Metadata
    Show full item record
    Abstract
    The temperature and pH dependence of the reaction of the superoxide radical anion with ferricytochrome c have been measured using the pulse-radiolysis technique. The temperature dependence of the reaction at low ionic strength yields an activation energy of 31 +/- 5 kJ/mol as compared to 14 +/- 3 kJ/mol for the reaction of CO2.(-) under the same conditions. The pH dependence fits the single pK'a of ferricytochrome c of 9.1. The bimolecular rate constant for the reaction of the superoxide anion with ferricytochrome c at pH 7.8, 21 +/- 2 degrees C, in the presence of 50 mM phosphate and 0.1 mM EDTA is (2.6 +/- 0.1) X 10(5) M-1 s-1. Using this value, 1 unit of superoxide dismutase activity (McCord, J. M., and Fridovich, I. (1969) J. Biol. Chem. 244, 6049-6055) is calculated to be 3.6 +/- 0.3 pmol of enzyme if the assay is performed in a total volume of 3.0 ml. Copper ions reduce the yield of the reaction of ferricytochrome c with CO2.(-). The reactivities of native and singly modified 4-carboxy-2,4-dinitrophenyllysine cytochromes c towards the superoxide anion radical are in the order native greater than 4-carboxy-2,4-dinitrophenyllysine 60 greater than lysine 13 greater than lysine 87 greater than lysine 27 greater than lysine 86 greater than lysine 72, indicating that electron transfer takes place at or close to the solvent accessible heme edge. The mechanism of the reaction is discussed in terms of the approach of superoxide anion radicals to the heme edge and the available molecular orbitals of both heme and free radicals.
    Citation
    Kinetics and mechanism of the reduction of ferricytochrome c by the superoxide anion. 1982, 257 (18):10747-50 J. Biol. Chem.
    Journal
    Journal of Biological Chemistry
    URI
    http://hdl.handle.net/10541/133510
    PubMed ID
    6286671
    Type
    Article
    Language
    en
    ISSN
    0021-9258
    Collections
    All Paterson Institute for Cancer Research

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