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AKB: Biologische Physik

AKB 50: Poster Session "Biological Physics"

AKB 50.63: Poster

Freitag, 12. März 2004, 10:30–13:00, B

Investigation of the N-terminal domain of LHCII using single molecule techniques — •Felix Neugart¹, Sebastian Schuler¹, Carsten Tietz¹, Jörg Wrachtrup¹, Stephanie Boggasch², and Manuel Lion² — ¹3. Physikalisches Institut, Universität Stuttgart — ²Institut für Allgemeine Botanik, Universität Mainz

The light-harvesting complex II (LHCII) is the most abundant chlorophyll-binding complex in photosynthesis of green plants. The native LHCII trimer is responsible for the absorption of half the photons involved in photosynthesis of algae and higher plants.

The structure of the transmembrane part of the protein of the LHCII is well known (Kühlbrandt et al. 1994, Nature 367, 614-621) whereas the N-terminal region of the LHCII complex is not resolved and its function, orientation and dynamic is still under debate.

One possibility to gather information about the motion of the N-terminal domain is to attach an artificial fluorophor to the N-terminus and observe the energy transfer to the Chlorophylls of the LHCII. Different conformations of the N-terminal domain lead to different energy transfer rates. Hence, the observation of single labeled LHCII-Monomers in a confocal setup monitors the dynamics of the N-terminal region and reveal subensembles of different conformations.