Intramolecular Electron Transfer in Peptides Containing Methionine, Tryptophan and Tyrosine: A Pulse Radiolysis Study

References

• Adams G.E., Aldrich J.E., Bisby R.H., Cundall R.B., Redpath J.L., Wilson R.L. Selective free radical reactions with proteins and enzymes: reaction of inorganic radical anions with amino acids. Radiation Research 1972; 49: 278–289
   PubMed Web of Science ®Google Scholar
• Axup A.W., Albin M., Mayo S.L., Crutchley R.J., Gray H.B. Distance dependence of photoinduced long-range electron transfer in zinc/rutheniummodified myoglobins. Journal of the American Chemical Society 1988; 110: 435–439
   Google Scholar
• Bobrowski K., Łubis R. Intermolecular charge transfer involving tryptophan, tyrosine, and three-electron-bonded intermediates derived from methionine. International Journal of Radiation Biology 1986; 50: 1039–1050
   Web of Science ®Google Scholar
• Bobrowski K., Wierzchowski K.L., Holcman J., Ciurak M. Intramolecular charge transfer between tryptophan and tyrosine in peptides with bridging prolines. Studia Biophysica 1987; 122: 23–28
   Google Scholar
• Butler J., Land E.J., Prütz W.A., Swallow A.J. Charge transfer between tryptophan and tyrosine in peptides. Biochimica et Biophysica Acta 1982; 705: 150–162
   Web of Science ®Google Scholar
• Butler J., Land E.J., Prütz W.A., Swallow A.J. Reversibility of charge transfer between tryptophan and tyrosine. Journal of the Chemical Society, Chemical Communications 1986; 348–349
   Google Scholar
• Chiu H., Bersohn R. Electronic energy transfer between tyrosine and tryptophan in the peptides Trp-(Pro)n-Tyr. Biopolymers 1977; 16: 277–288
   Google Scholar
• Creighton T.E. Proteins. Structures and Molecular Properties1st edn. W. H. Freeman, New York 1984; 160–163
   Google Scholar
• DeVault D. Quantum-Mechanical Tunneling in Biological Systems2nd edn. Cambridge University Press, Cambridge 1984
   Google Scholar
• Evans R.F., Ghiron C.A., Volkert W.A., Kuntz R.R., Santus R., Bazin M. Flash photolysis of N-acetyl-l-tryptophanamide; acid-base equilibrium of radical transients. Chemical Physics Letters 1976; 42: 43–45
   Web of Science ®Google Scholar
• Faraggi M., Klapper M.H. Intramolecular long-range electron transfer in the α-hemoglobin unit. Journal of the American Chemical Society 1988; 110: 5753–5756
   Google Scholar
• Faraggi M., De Felippis M.R., Klapper M.H. Long-range electron transfer between tyrosine and tryptophan in peptides. Journal of the American Chemical Society 1989; 111: 5141–5145
   Google Scholar
• Grathwohl C., Wüthrich K. The X-Pro peptide bond as a nmr probe for conformational studies of flexible linear peptides. Biopolymers 1976; 15: 2025–2041
   PubMed Web of Science ®Google Scholar
• Harriman A. Further comments on the redox potentials of tryptophan and tyrosine. Journal of Physical Chemistry 1987; 91: 6102–6104
   Web of Science ®Google Scholar
• Helbecque N., Loucheux-Lefebvre M.H. Critical chain length for polyproline-II structure formation in H-(Gly)-(Pro)n-OH. International Journal of Peptide and Protein Research 1982; 19: 94–101
   Google Scholar
• Hiller K.-O., Asmus K.-D. Oxidation of methionine by X-·2 in aqueous solution and characterization of some > ∴X three-electron-bonded intermediates. A pulse radiolysis study. International Journal of Radiation Biology 1981; 40: 583–595
   Web of Science ®Google Scholar
• Isied S.S., Vassilian A. Electron transfer across polypeptides. 3. Oligoproline bridging ligands. Journal of the American Chemical Society 1984; 106: 1732–1736
   Google Scholar
• Isied S.S., Vassilian A., Magnusson R.H., Schwarz H.A. Electron transfer across peptides. 5. Rapid rates of electron transfer between Os(II) and Co(III) in complexes with bridging oligoprolines and other polypeptides. Journal of the American Chemical Society 1985; 107: 7432–7438
   Web of Science ®Google Scholar
• Isied S.S., Vassilian A., Wishart J.F., Creutz C., Schwarz H.A., Sutin N. The distance dependence of intramolecular electron-transfer rates: importance of the nuclear factor. Journal of the American Chemical Society 1988; 110: 635–637
   Web of Science ®Google Scholar
• Karolczak S., Hodyr K., Łubis R., Kroh J. Pulse radiolysis system based on ELU-6 LINAC. Journal of Radioanalytical and Nuclear Chemistry 1986; 101: 177–188
   Web of Science ®Google Scholar
• Land E.J., Prütz W.A. Fast one-electron oxidation of tryptophan by azide radicals. International Journal of Radiation Biology 1977; 32: 203–207
   Web of Science ®Google Scholar
• Land E.J., Prütz W.A. Reaction of azide radicals with amino acids and proteins. International Journal of Radiation Biology 1979; 36: 75–83
   Web of Science ®Google Scholar
• Marcus R.A., Sutin N. Electron transfer in chemistry and biology. Biochimica et Biophysica Acta 1985; 811: 265–322
   Web of Science ®Google Scholar
• McLendon G.L., Miller J.R. The dependence of biological electron transfer rates on exothermicity: The cytochrome c/cytochrome b5 couple. Journal of the American Chemical Society 1985; 107: 7811–7816
   Web of Science ®Google Scholar
• Newton M.D., Sutin N. Electron transfer reactions in condensed phases. Annual Review of Physical Chemistry 1984; 35: 437–480
   Web of Science ®Google Scholar
• Perrin D.D. Dissociation Constants of Organic Bases in Aqueous Solution. UPAC-Butterworth, London 1965
   Google Scholar
• Prütz W.A. Radical transformations in peptides and proteins. Radiation Research. 8th International Congress of Radiation Research, Edinburgh. E.M. Fielden, J.F. Fowler, J.H. Hendry, D. Scott. Taylor and Francis, London 1987; 2: 134–139
   Google Scholar
• Prütz W.A., Land E.J. Charge transfer in peptides. Pulse radiolysis investigation of one-electron reactions in dipeptides of tryptophan and tyrosine. International Journal of Radiation Biology 1979; 36: 513–520
   Web of Science ®Google Scholar
• Prütz W.A., Land E., Sloper R.W. Charge transfer in peptides. Journal of the Chemical Society, Faraday Transactions I 1981; 77: 281–292
   Google Scholar
• Prütz W.A., Siebert F., Butler J., Land E.J., Menez A., Montenay-Garestier T. Intramolecular radical transformations involving methionine, tryptophan, and tyrosine. Biochimica et Biophysica Acta 1982; 705: 139–149
   Web of Science ®Google Scholar
• Prütz W.A., Butler J., Land E.J. Phenol coupling initiated by one-electron oxidation of tyrosine units in peptides and histone. International Journal of Radiation Biology 1983; 44: 183–196
   Web of Science ®Google Scholar
• Prütz W.A., Butler J., Land E.J. Methionyl→tyrosyl radical transitions initiated by Br-2 in peptide model systems and ribonuclease A. International Journal of Radiation Biology 1985; 47: 149–156
   Web of Science ®Google Scholar
• Prütz W.A., Butler J., Land E.J., Swallow A.J. Unpaired electron migration between aromatic and sulphur peptide units. Free Radical Research Communications 1986; 2: 69–75
   PubMedGoogle Scholar
• Ramachandran G.N., Sasisekharan V. Conformation of polypeptide and proteins. Advances in Protein Chemistry 1968; 23: 283–437
   PubMedGoogle Scholar
• Schanze K.S., Sauer K. Photoinduced intramolecular electron transfer in peptide bridged molecules. Journal of the American Chemical Society 1988; 110: 1180–1186
   Web of Science ®Google Scholar
• Schiller P.W. The Peptides, S. Udenfriend, J. Meinhofer. Academic Press, New York 1984; 6: 219–268
   Google Scholar
• Sehested K., Holcman J., Hart E.J. Rate constants and products of the reactions of e-aq, O-2 and H with ozone in aqueous solutions. Journal of Physical Chemistry 1983; 87: 1951–1954
   Web of Science ®Google Scholar
• Stryer L., Haugland R.P. Energy transfer: A spectroscopic ruler. Proceedings of the National Academy of Sciences U.S.A. 1967; 58: 719–726
   PubMed Web of Science ®Google Scholar
• Sutin N. Nuclear, electronic, and frequency factors in electron-transfer reactions. Accounts of Chemical Research 1982; 9: 275–282
   Google Scholar