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MO: Molekülphysik
MO 27: Poster: Femtosecond Spectroscopy
MO 27.7: Poster
Dienstag, 14. März 2006, 16:30–18:30, Labsaal
Trans-cis reaction dynamics in sensory rhodpsin II by femtosecond time-resolved IR spectroscopy: protein and chromophore dynamics — •Ruth Jakober1, Christian Schumann1, Rolf Diller1, Johann P. Klare2, and Martin Engelhard2 — 1Fachbereich Physik, Technische Universität Kaiserslautern, 67663 Kaiserslautern — 2Max-Planck-Institut f. Molekulare Physiologie, 44227 Dortmund
Transient vibrational spectroscopy, which provides insights into processes associated with protein-based photoreactions such as structural changes of the chromophore, its vibrational relaxation and the dynamics of the protein environment, has been performed on sensory rhodopsin II from Natronomonas pharaonis at sub-picosecond time resolution.
We present new data on the dynamics of the chromophore and the surrounding protein due to the primary all-trans to 13-cis retinal photoisomerization. Three time constants (0.5 ps, 4 ps ans 11 ps) were obtained [1]. It was found that the isomerization takes place within 0.5 ps, followed by an electronic ground state relaxation (4 ps) which corresponds to experiments in the visible spectral region. The 11 ps time constant is discussed as an indication of protein dynamics or a vibrational cooling process.
[1] Rolf Diller, Ruth Jakober, Christian Schumann, Frank Peters, Johann P. Klare, Martin Engelhard; Biopolymers: Biophysics, submitted 2005.