Time resolved CIDNP study of electron transfer reactions in proteins and model compounds

Conference item

Intramolecular electron transfer (IET) from tyrosine to tryptophan cation radicals is investigated using time resolved chemically induced dynamic nuclear polarization (CIDNP) spectroscopy in combination with laser flash photolysis. In both the tryptophan-tyrosine dipeptide and the denatured state of hen lysozyme in aqueous solution, the transformation TrpH+. → TyrO. by IET leads to an increase in the tyrosine radical concentration, growth in the tyrosine CIDNP signal, fast decay of the tryptophan CIDNP, and inversion of the phase of the CIDNP of the photosensitizing dye, 2,2′-dipyridyl. IET effects are not observed for mixtures of the amino acid or for the native state of lysozyme. The steady state CIDNP effects seen for denatured lysozyme thus depend not only on the accessibility of the amino acid residues on the surface of the protein but also on the reactivity of the radical intermediates.

Authors: Morozova, O; Yurkovskaya, A; Tsentalovich, Y; Forbes, M; Hore, P

• Publication status: Published
• Host title: MOLECULAR PHYSICS
• Volume: 100
• Issue: 8
• Pages: 1187-1195
• Publication date: 2002-04-01
• DOI: 10.1080/00268970110109970
• EISSN: 1362-3028
• ISSN: 0026-8976