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Proceedings Paper

Specific molecular aggregation of photosynthetic pigment-protein complex LHCII
Author(s): Wieslaw I. Gruszecki; Ewa Janik; Wojciech Grudzinski; Peter Kernen; Malgorzata Gospodarek; Waldemar Maksymiec; Zbigniew Krupa
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Paper 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.

Paper Details

Date Published: 21 February 2008
PDF: 8 pages
Proc. SPIE 6862, Single Molecule Spectroscopy and Imaging, 68620W (21 February 2008); doi: 10.1117/12.761718
Show Author Affiliations
Wieslaw I. Gruszecki, Maria Curie-Sklodowska Univ. (Poland)
Ewa Janik, Maria Curie-Sklodowska Univ. (Poland)
Wojciech Grudzinski, Maria Curie-Sklodowska Univ. (Poland)
Peter Kernen, Zyomyx Inc. (United States)
Malgorzata Gospodarek, Lublin Technical Univ. (Poland)
Waldemar Maksymiec, Maria Curie-Sklodowska Univ. (Poland)
Zbigniew Krupa, Maria Curie-Sklodowska Univ. (Poland)

Published in SPIE Proceedings Vol. 6862:
Single Molecule Spectroscopy and Imaging
Jörg Enderlein; Zygmunt K. Gryczynski; Rainer Erdmann, Editor(s)

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