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