Carotenoid S1 State in a Recombinant Light-Harvesting Complex of Photosystem II
- 15 December 2001
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 41 (2), 439-450
- https://doi.org/10.1021/bi011589x
Abstract
The carotenoid species lutein, violaxanthin, and zeaxanthin are crucial in the xanthophyll-dependent nonphotochemical quenching occurring in photosynthetic systems of higher plants, since they are involved in dissipation of excess energy and thus protect the photosynthetic machinery from irreversible inhibition. Nonetheless, important properties of the xanthophyll cycle carotenoids, such as the energy of their S1 electronic states, are difficult to study and were only recently determined in organic solvents [Polívka, T. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 4914. Frank, H. A. (2000) Biochemistry 39, 2831]. In the present study, we have determined the S1 energies of three carotenoid species, violaxanthin, lutein, and zeaxanthin, in their LHCII (peripheral light-harvesting complex of photosystem II) protein environment by constructing recombinant Lhcb1 (Lhc = light-harvesting complex) proteins containing single carotenoid species. Within experimental error the S1 energy is the same for all three carotenoids in the monomeric LHCII, 13900 ± 300 cm-1 (720 ± 15 nm), thus well below the Qy transitions of chlorophylls. In addition, we have found that, although the S1 lifetimes of violaxanthin, lutein, and zeaxanthin differ substantially in solution, when incorporated into the LHCII protein, their S1 states have in fact the same lifetime of about 11 ps. Despite the similar spectroscopic properties of the carotenoids bound to the LHCII, we observed a maximal fluorescence quenching when zeaxanthin was present in the LHCII complex. On the basis of these observations, we suggest that, rather than different photochemical properties of individual carotenoid species, changes in the protein conformation induced by binding of carotenoids with distinct molecular structures are involved in the quenching phenomena associated with Lhc proteins.This publication has 21 references indexed in Scilit:
- Carotenoid-to-Chlorophyll Energy Transfer in Recombinant Major Light-Harvesting Complex (LHCII) of Higher Plants. I. Femtosecond Transient Absorption MeasurementsBiophysical Journal, 2001
- Understanding the Energy Transfer Function of LHCII, the Major Light-Harvesting Complex of Green PlantsThe Journal of Physical Chemistry B, 2000
- Identifying the Pathways of Energy Transfer between Carotenoids and Chlorophylls in LHCII and CP29. A Multicolor, Femtosecond Pump−Probe StudyThe Journal of Physical Chemistry B, 2000
- Two-Photon Excitation Spectrum of Light-Harvesting Complex II and Fluorescence Upconversion after One- and Two-Photon Excitation of the CarotenoidsThe Journal of Physical Chemistry B, 2000
- Ultrafast Energy Transfer in LHC-II Revealed by Three-Pulse Photon Echo Peak Shift MeasurementsThe Journal of Physical Chemistry B, 2000
- Xanthophyll Cycle Pigment Localization and Dynamics during Exposure to Low Temperatures and Light Stress inVinca major1Plant Physiology, 1999
- Determination of the Stoichiometry and Strength of Binding of Xanthophylls to the Photosystem II Light Harvesting ComplexesJournal of Biological Chemistry, 1999
- Solvent Dependence of the Ultrafast S2−S1 Internal Conversion Rate of β-CaroteneThe Journal of Physical Chemistry A, 1998
- Ultrafast Spectroscopy of Trimeric Light-Harvesting Complex II from Higher PlantsThe Journal of Physical Chemistry B, 1997
- Carotenoid‐binding proteins of photosystem IIEuropean Journal of Biochemistry, 1993