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Berlin 2001 – wissenschaftliches Programm

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CPP: Chemische Physik und Polymerphysik

CPP 17: Poster: Spectroscopy and Single Particle Spectroscopy of Molecular Systems, Photoprocesses, Biological Systems

CPP 17.24: Poster

Dienstag, 3. April 2001, 12:30–15:00, AT1

A first-principles study of 11-cis retinal: Modelling the chromophore-protein interaction in rhodopsin — •Sugihara Minoru1, Entel Peter1, and Buss Volker21Theoretical Physics, University of Duisburg, Germany — 2Theoretical Chemistry, University of Duisburg, Germany

The 11-cis-retinal protonated Schiff base is the chromophore of rhodopsin, the photoreceptor in the eye. The photochemical isomerization from 11-cis to the all-trans form triggers a series of enzymatic reactions known as the visual cascade which eventually leads to a neural signal. Experiments such as resonance Raman, NMR etc., have shown that 11-cis-retinal is probably highly twisted in the protein pocket. Because detailed knowledge about the kind of interaction with the protein is missing, a theoretical description of the chromophore conformation is difficult. In the simulations the results of which will be presented here, we assume that the retinal chromophore, as a consequence of the steric fit into the protein binding pocket, undergoes a specific kind of conformational change. The structure we obtain is in good agreement with the experimentally observed highly twisted conformation of the chromophore backbone.
V. Buss, O. Weingart, and M. Sugihara, Angew. Chem. Int. Ed. 39 (2000) 2784.

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