Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 116, Issue 12, Pages 3834-3849Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp210042z
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Funding
- National Science Foundation [MCB-0913022]
- University of Connecticut Research Foundation
- Italian Ministry of Research [2008XB774B]
- EU [PITN-GA-2009-238017 1030 HARVEST]
- Czech Ministry of Education [ME09037]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0913022] Funding Source: National Science Foundation
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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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