BIPHOTONIC PROCESSES IN PROTEINS: COMPARATIVE STUDIES OF DELAYED FLUORESCENCE AND ISOTHERMAL OR OPTICALLY STIMULATED RECOMBINATION LUMINESCENCE |
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| Authors: | M. Bazin M. Aubailly R. Santus |
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| Affiliation: | Laboratoire de Biophysique, Muséum National d'Histoire Naturelle, 61, Rue Buffon 75005 Paris, France |
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| Abstract: | Abstract —The properties of delayed fluorescence (DF) of proteins are studied in parallel with their properties of recombination luminescence, produced after ultraviolet excitation and photoionization of chromophoric residues at low temperature, in water-ethylene glycol glasses. It is shown that the DF emission of proteins, originating from tryptophan residues, is produced via triplet-triplet absorption processes, photoionization of tryptophan residues, and recombination of the charged species. Electron scavengers that reduce the DF yield act differently upon the DF emission and the recombination luminescence as a consequence of the protein structure. Influence of energy transfer on the protein DF yield is also emphasized. |
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