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Role of Xanthophylls in Light Harvesting in Green Plants: A Spectroscopic Investigation of Mutant LHCII and Lhcb Pigment–Protein Complexes

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Department of Chemistry, University of Connecticut, U-3060, 55 North Eagleville Road, Storrs, Connecticut 06269-3060, United States
Institute of Physical Biology, University of South Bohemia, Nove Hrady, Czech Republic
§ Dipartimento di Biotecnologie, Università di Verona, Strada Le Grazie 15, I-37134 Verona, Italy
Cite this: J. Phys. Chem. B 2012, 116, 12, 3834–3849
Publication Date (Web):February 28, 2012
Copyright © 2012 American Chemical Society

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    The spectroscopic properties and energy transfer dynamics of the protein-bound chlorophylls and xanthophylls in monomeric, major LHCII complexes, and minor Lhcb complexes from genetically altered Arabidopsis thaliana plants have been investigated using both steady-state and time-resolved absorption and fluorescence spectroscopic methods. The pigment–protein complexes that were studied contain Chl a, Chl b, and variable amounts of the xanthophylls, zeaxanthin (Z), violaxanthin (V), neoxanthin (N), and lutein (L). The complexes were derived from mutants of plants denoted npq1 (NVL), npq2lut2 (Z), aba4npq1lut2 (V), aba4npq1 (VL), npq1lut2 (NV), and npq2 (LZ). The data reveal specific singlet energy transfer routes and excited state spectra and dynamics that depend on the xanthophyll present in the complex.

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    SDS-PAGE analyses of the polypeptide composition of Lhcb and LHCII complexes, percentage of antenna proteins in the samples, transient absorption spectra of LHCII complexes from mutants containing V, N, NVL (wild type), NV, VL, and LZ in the visible and NIR spectral region after 676 or 490 nm excitation, and evolution associated differential spectra of Lhcb and LHCII complexes from mutants containing NVL, NV, VL, and LZ in the visible and NIR spectral region after 676 or 490 nm excitation. This material is available free of charge via the Internet at

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