Ephemerals, widely distributed in the Gobi desert, have developed significant characteristics to sustain high photosynthetic efficiency under high light (HL) conditions. Since the light reaction is the basis for photosynthetic conversion of solar energy to chemical energy, the photosynthetic performances in thylakoid membrane of the spring ephemerals in response to HL were studied. Three plant species, namely two C3 spring ephemeral species of Cruciferae: Arabidopsis pumila (A. pumila) and Sisymbrium altissimum (S. altissimum), and the model plant Arabidopsis thaliana (A. thaliana) were chosen for the study. The ephemeral A. pumila, which is genetically close to A. thaliana and ecologically in the same habitat as S. altissimum, was used to avoid complications arising from the superficial differences resulted from comparing plants from two extremely contrasting ecological groups. The findings manifested that the ephemerals showed significantly enhanced activities of photosystem (PS) II under HL conditions, while the activities of PSII in A. thaliana were markedly decreased under the same conditions. Detailed analyses of the electron transport processes revealed that the increased plastoquinone pool oxidization, together with the enhanced PSI activities, ensured a lowered excitation pressure to PSII of both ephemerals, and thus facilitated the photosynthetic control to avoid photodamage to PSII. The analysis of the reaction centers of the PSs, both in terms of D1 protein turnover kinetics and the long-term adaptation, revealed that the unusually stable PSs structure provided the basis for the ephemerals to carry out high photosynthetic performances. It is proposed that the characteristic photosynthetic performances of ephemerals were resulted from effects of the long-term adaptation to the harsh environments.

The light-harvesting chlorophyll a/b-binding protein of photosystem II (LHCIIb) fulfills multiple functions, such as light harvesting and energy dissipation under different illuminations. The crystal structure of LHCIIb at the near atomic resolution reveals an antiparallel strands structure in the lumenal loop between the transmembrane helices B/C. To study the structural and functional significances of this structure, three amino acids (Val-119, His-120, and Ser-123) in this region have been exchanged to Phe, Leu, and Gly, respectively, and the influence of the mutagenesis on the structure and function of LHCIIb has been investigated. The results are as follows. 1) Circular dichroism spectra of the mutations reveals that the antiparallel strands in the lumenal region are very important for adjusting pigment conformation in the neoxanthin domain of LHCIIb. Although the mutagenesis causes only a slight loss of the Neo binding in the complexes (V119F, 0.09; S123G, 0.19; and H120L, 0.27), it imparts remarkable changes to the pigment conformation. 2) Substituting Ser-123 with Gly results in a higher susceptibility to photodamage, an increased tendency to aggregate, and enhanced fluorescence quenching induced by the medium acidification. These results demonstrate that this antiparallel strands domain plays an important role in regulating the pigment conformation and in adjusting the aggregation and the fluorescence yield of LHCIIb.

The major light-harvesting chlorophyll (Chl) a/b complexes of photosystem II (LHCIIb) play important roles in energy balance of thylakoid membrane. They harvest solar energy, transfer the energy to the reaction center under normal light condition and dissipate excess excitation energy under strong light condition. Many bamboo species could grow very fast even under extremely changing light conditions. In order to explain whether LHCIIb in bamboo contributes to this specific characteristic, the spectroscopic features, the capacity of forming homotrimers and structural stabilities of different isoforms (Lhcb1-3) were investigated. The apoproteins of the three isoforms of LHCIIb in bamboo are overexpressed in vitro and successfully refolded with thylakoid pigments. The sequences of Lhcb1 and Lhcb2 are similar and they are capable of forming homotrimer, while Lhcb3 lacks 10 residues in the N terminus and can not form the homotrimeric structure. The pigment stoichiometries, spectroscopic characteristics, thermo- and photostabilities of different reconstituted Lhcbs reveal that Lhcb3 differs strongly from Lhcb1 and Lhcb2. Lhcb3 possesses the lowest Qy transition energy and the highest thermostability. Lhcb2 is the most stable monomer under strong illumination among all the isoforms. These results suggest that in spite of small differences, different Lhcb isoforms in bamboo possess similar characteristics as those in other higher plants.