Tyrosine residues (Tyr) on proteins are a favoured site of one-electron oxidation due to their low one-electron reduction potentials. In this work, light-induced oxidation of Tyr residues was investigated using direct ionisation (via 266 nm light excitation) and sensitized photo-oxidation (by 3-carboxybenzophenone as sensitizer and 355 nm). Light emission (fluorescence) was observed at 410-440 nm as a result of Tyr oxidation. This novel light emission process is shown to be dependent on the solvent and aromatic ring substituents, however it does not depend on pH. It is proposed, that after initial formation of tyrosine phenoxyl radicals (TyrO●) by one electron-oxidation, the TyrO● absorbs a second photon to give an excited state species that undergoes subsequent light emission. The intensity of this emission depends on the Tyr concentration, and the detection of this emission can be used to identify and quantify one-electron formation of oxidized Tyr residues on proteins.
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