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Fluorescent Derivatives of the GFP Chromophore Give a New Insight into the GFP Fluorescence Process

Anny Follenius-Wund ^*, Maryline Bourotte , Martine Schmitt , Fatih Iyice ^*, Hans Lami ^*, Jean-Jacques Bourguignon , Jacques Haiech ^* and Claire Pigault ^*

^* UMR CNRS 7034-Pharmacologie et Physico-Chimie des Interactions Cellulaires et Moléculaires, and UMR CNRS 7081-Laboratoire de Pharmacochimie de la Communication Cellulaire, Université Louis Pasteur Strasbourg I, Faculté de Pharmacie, BP 24, 67401 Illkirch-Cedex, France

Correspondence: Address reprint requests to Jacques Haiech, E-mail: haiech{at}ecs.u-strasbg.fr.

The photophysical properties of synthetic compounds derived from the imidazolidinone chromophore of the green fluorescent protein were determined. Various electron-withdrawing or electron-donating substituents were introduced to mimic the effect of the chromophore surroundings in the protein. The absorption and emission spectra as well as the fluorescence quantum yields in dioxane and glycerol were shown to be highly dependent on the electronic properties of the substituents. We propose a kinetic scheme that takes into account the temperature-dependent twisting of the excited molecule. If the activation energy is low, the molecule most often undergoes an excited-state intramolecular twisting that leads it to the ground state through an avoided crossing between the S₁ and S₀ energy surfaces. For a high activation energy, the torsional motion within the compounds is limited and the ground-state recovery will occur preferentially by fluorescence emission. The excellent correlation between the fluorescence quantum yields and the calculated activation energies to torsion points to the above-mentioned avoided crossing as the main nonradiative deactivation channel in these compounds. Finally, our results are discussed with regard to the chromophore in green fluorescent protein and some of its mutants.

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