Specific molecular aggregation of photosynthetic pigment-protein complex LHCII

Wieslaw I. Gruszecki; Ewa Janik; Wojciech Grudzinski; Peter Kernen; Malgorzata Gospodarek; Waldemar Maksymiec; Zbigniew Krupa

doi:10.1117/12.761718

21 February 2008 Specific molecular aggregation of photosynthetic pigment-protein complex LHCII

Wieslaw I. Gruszecki, Ewa Janik, Wojciech Grudzinski, Peter Kernen, Malgorzata Gospodarek, Waldemar Maksymiec, Zbigniew Krupa

Author Affiliations +

Proceedings Volume 6862, Single Molecule Spectroscopy and Imaging; 68620W (2008) https://doi.org/10.1117/12.761718
Event: SPIE BiOS, 2008, San Jose, California, United States

Abstract

LHCII is a largest plant photosynthetic antenna complex. Examination of monomolecular layers of LHCII. with Atomic Force Microscopy reveals formation of regular ring-like structures composed of six trimers of the complex. FTIR analysis of aggregated LHCII suggests that regular supramolecular structures of the complex are stabilized by hydrogen bonding between the α helices C of neighboring trimers. Analysis of fluorescence emission spectra of LHCII-bound chlorophyll a reveals that the aggregation is associated with formation of new electronic energy levels that can be particularly important for both photosynthetic excitation energy transfer and quenching of excessive excitations under overexcitation conditions.

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Wieslaw I. Gruszecki, Ewa Janik, Wojciech Grudzinski, Peter Kernen, Malgorzata Gospodarek, Waldemar Maksymiec, and Zbigniew Krupa "Specific molecular aggregation of photosynthetic pigment-protein complex LHCII", Proc. SPIE 6862, Single Molecule Spectroscopy and Imaging, 68620W (21 February 2008); https://doi.org/10.1117/12.761718

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