Berlin 2008 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 5: Photobiophysics
BP 5.3: Vortrag
Montag, 25. Februar 2008, 16:45–17:00, PC 203
Chlorophyll binding protein complexes: Nanostructure and optical properties — •Franz-Josef Schmitt1, Christoph Theiss1, Gernot Renger2, and Hans Joachim Eichler1 — 1Institut für Optik und Atomare Physik — 2Max Volmer Laboratorium TU Berlin, Strasse des 17. Juni 135, 10623 Berlin
The photophysical and biochemical properties of pigments change due to surrounding protein environments. This principle has been perfectly in the biosphere. Photosynthetic organisms developed pigment-protein complexes for efficient light collection, transfer of electronically excited states and transformation into electrochemical free energy. In addition to the photosynthetic apparatus plants contain also water soluble chlorophyll (Chl) binding proteins (WSCPs) which most likely exert not yet clarified regulatory functions. A striking feature -among several interesting properties-is the retardation of the formation of highly reactive singlet oxygen in WSCP. Although the origin of this effect is not yet clarified, it seems likely that the protein matrix is able to diminish the sensitized reaction of bound chlorophyll with the surrounding oxygen.
A wide range of linear and non-linear optical techniques have been used to determine successfully the properties of these pigment protein complexes providing a deeper understanding of the influence of protein interactions on the electronic structure of the pigments. Time resolved fluorescence spectroscopy combined with two photon excitation will help to investigate the pigment interactions directly in biological tissues.