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Biophysical Journal 88:2779-2788 (2005)
© 2005 The Biophysical Society

Ultrafast Excited State Dynamics of the Protonated Schiff Base of All-trans Retinal in Solvents

Goran Zgrablic *, Kislon Voïtchovsky *, Maik Kindermann {dagger}, Stefan Haacke * and Majed Chergui *

* Laboratoire de Spectroscopie Ultrarapide and {dagger} Laboratory of Protein Engineering, Ecole Polytechnique Fédérale de Lausanne, Institute of Chemical Sciences and Engineering, FSB-BSP, CH-1015 Lausanne-Dorigny, Switzerland

Correspondence: Address reprint requests to Stefan Haacke, E-mail: stefan.haacke{at}ipcms.u-strasbg.fr.

We present a comparative study of the ultrafast photophysics of all-trans retinal in the protonated Schiff base form in solvents with different polarities and viscosities. Steady-state spectra of retinal in the protonated Schiff base form show large absorption-emission Stokes shifts (6500–8100 cm–1) for both polar and nonpolar solvents. Using a broadband fluorescence up-conversion experiment, the relaxation kinetics of fluorescence is investigated with 120 fs time resolution. The time-zero spectra already exhibit a Stokes-shift of ~6000 cm–1, indicating depopulation of the Franck-Condon region in ≤100 fs. We attribute it to relaxation along skeletal stretching. A dramatic spectral narrowing is observed on a 150 fs timescale, which we assign to relaxation from the S2 to the S1 state. Along with the direct excitation of S1, this relaxation populates different quasistationary states in S1, as suggested from the existence of three distinct fluorescence decay times with different decay associated spectra. A 0.5–0.65 ps decay component is observed, which may reflect the direct repopulation of the ground state, in line with the small isomerization yield in solvents. Two longer decay components are observed and are attributed to torsional motion leading to photo-isomerization. The various decay channels show little or no dependence with respect to the viscosity or dielectric constant of the solvents. This suggests that in the protein, the bond selectivity of isomerization is mainly governed by steric effects.




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