Regensburg 2010 – scientific programme
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BP: Fachverband Biologische Physik
BP 29: Biomolecular Spectroscopy
BP 29.6: Talk
Thursday, March 25, 2010, 16:00–16:15, H45
Pigment fluorescence in protein environment — •Franz-Josef Schmitt1, Heinrich Südmeyer2, Kai Reineke1, Insa Kahlen1, Joachim Börner1, Max Schoengen1, Patrick Hätti1, Hans Joachim Eichler1, and Hans-Joachim Cappius2 — 1Berlin Institute of Technology, Berlin — 2Laser- und Medizintechnologie GmbH, Berlin
The electronic properties of organic molecules strongly depend on the local environment. Therefore it is difficult to detect specific molecules if the environment of the molecules is not clearly defined. On the other hand the fine tunig of the local protein environment leads to specific pathways for excitation energy migration between pigments in e.g. photosynthetic plant complexes and the influence of the environment is essential for the light harvesting functionality. In this study we compare the time resolved fluorescence of pigments (e.g. fluorescein, chlorophyll) and pigment protein complexes (e.g. Bovine serum albumin, water soluble chlorophyll binding protein and photosynthetic light harvesting complexes). The protein matrix has an own characteristic influence onto the chromophores and strongly diminishes the environmental influence onto the chromophores. The fluorescence of fluoresceine and chlorophylle molecules on glass surface is strongly quenched while the pigments bound to protein complexes show only slight changes of the fluorescence dynamics due to the surface contact.
Financial support by DFG project SfB 429 and Federal Ministry of Education and Research (BMBF) is greatfully acknowledged.