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    Methionyl----tyrosyl radical transitions initiated by Br2-. in peptide model systems and ribonuclease A.

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    Authors
    Prütz, W A
    Butler, John
    Land, Edward J
    Affiliation
    Universitat Freiburg, Institut fur Biophysik und Strahlenbiologie, Albertstr. 23, D-7800 Freiburg, F.R. Germany.
    Issue Date
    1985-02
    
    Metadata
    Show full item record
    Abstract
    A series of radical transitions, Br2-.----Met(S therefore Br)----Trp(indolyl)----Tyr (phenoxyl), has been demonstrated by pulse radiolysis of N2O-saturated aqueous solutions containing Br-, Met-Gly and Trp-(Gly)2-Tyr at pH 6.7. The intramolecular Met(S therefore Br)----Trp(indolyl) transition in the dipeptide Met-Trp is shown to proceed via the Trp+. radical cation, with a rate constant of k approximately 10(7)s-1, consistent with an electron transfer. Br2-.-attack upon ribonuclease A (RNase) leads to a fast Met(S therefore Br)----Tyr(phenoxyl) process, k = (4.0 +/- 1.0) X 10(5)s-1, probably involving the solvent-exposed Met-29 and the adjacent Tyr-25. Phenoxyl dimerization in the RNase system produces the characteristic o,o'-biphenol fluorescence, but a competing interaction of the Tyr-25(phenoxyl) with the 26-84 disulphide group also appears possible.
    Citation
    Methionyl----tyrosyl radical transitions initiated by Br2-. in peptide model systems and ribonuclease A. 1985, 47 (2):149-56 Int J Radiat Biol Relat Stud Phys Chem Med
    Journal
    International Journal of Radiation Biology and Related Studies in Physics, Chemistry, and Medicine
    URI
    http://hdl.handle.net/10541/117151
    PubMed ID
    3872270
    Type
    Article
    Language
    en
    ISSN
    0020-7616
    Collections
    All Paterson Institute for Cancer Research

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