Summary
The aim of this chapter is to show how spectroscopic techniques, especially resonance Raman spectroscopy, have been used to characterize the structure of plant light-harvesting proteins in vitro and in vivo – revealing in particular changes in the conformation of these proteins upon induction of non-photochemical quenching of chlorophyll fluorescence (NPQ). Firstly, we will show that the major light-harvesting protein in higher plants can exist in at least two functionally different states, with a different conformation in the crystal form (as well as upon aggregation) from that in solution. Thus this protein can switch from a state where it harvests and transfers light energy with high efficiency (as is the case for the protein in solution), to a quenched, energy-dissipating state (in the crystal or aggregated form). These results led us to propose a role for this protein in photoprotection. After summarizing these in vitro results, we will explain how similar measurements in chloroplasts and whole leaves confirmed that these conformational changes were also seen in vivo, correlating with NPQ. Finally, we will present a model to explain our conclusions and will, furthermore, introduce some of the more recent advances in this field involving multi-molecular photosystem II architectures.
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Abbreviations
- Chl:
-
– Chlorophyll;
- FLIM:
-
– Fluorescence lifetime imaging;
- LHC:
-
– Family of related light-harvesting trans-membrane proteins in oxygenic photosynthetic organisms;
- LHCII:
-
– Major LHC of photosystem II;
- NPQ:
-
– Non-photochemical quenching of chlorophyll fluorescence;
- VAZ:
-
– Enzymatic cycle of interconversions between the xanthophylls violaxanthin, antheraxanthin and zeaxanthin. Operation of the cycle correlates with changes in NPQ;
- ν1–4 :
-
– Four main groups of bands in vibrational spectra of carotenoids
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Acknowledgments
This work was supported by EU program Marie Curie (FP7 Initial Training Network HARVEST), the ERC funding agency (PHOTPROT project), the French National Research Agency (ANR, Cyanoprotect Project), and by The Royal Society and BBSRC of the UK.
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Pascal, A.A., Ruban, A.V., Robert, B. (2014). Antenna Protein Conformational Changes Revealed by Resonance Raman Spectroscopy. In: Demmig-Adams, B., Garab, G., Adams III, W., Govindjee, . (eds) Non-Photochemical Quenching and Energy Dissipation in Plants, Algae and Cyanobacteria. Advances in Photosynthesis and Respiration, vol 40. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-9032-1_10
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