Journal
CHEMICAL PHYSICS
Volume 357, Issue 1-3, Pages 113-119Publisher
ELSEVIER
DOI: 10.1016/j.chemphys.2008.10.052
Keywords
Lhcb4; FRET; Rhodamine; PSII; Photosystem II; Phosphorylation; npq; Photoprotection
Funding
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO)
- FOM
- Experimental Plant Sciences
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The photosynthetic minor antenna complex CP29 of higher plants was singly mutated, overexpressed in Escherichia coli, selectively labeled with the fluorescent dye TAMRA at three positions in the N-terminal domain, and reconstituted with its natural pigments. Picosecond fluorescence experiments revealed rapid excitation energy transfer (similar to 20 ps) from TAMRA covalently attached to a cysteine at either position 4 or 97 (near file beginning and end of the N-terminal domain) to the chlorophylls in the hydrophobic part of the protein. This indicates that the N-terminus is folded back on the hydrophobic core. In 20% of the complexes, efficient transfer was lacking, indicating that the N-terminus can adopt different conformations. Time-resolved polarized fluorescence measurements demonstrate that the non-transferring conformations only allow restricted rotational motion of the dye molecule. When TAMRA was attached to a cysteine at position 40, the overall transfer efficiency was far lower, reflecting a larger distance to the hydrophobic region. (C) 2008 Elsevier B.V. All rights reserved.
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