Effects of different aggregation forms of LHC Ⅱ from Bryopsis corticulans on the excited state properties of Chl a

Effects of different aggregatio forms of LHC II from Bryopsis corticulans on the excited state properties of Chl a

Steady-state and time-resolved fluo- rescence spectroscopies have been used to study the excited state properties of Chl a in different ag- gregation forms of light-harvesting complex II (LHC II) from an intertidal green alga, Bryopsis corticulans, i.e. LHC II monomer, trimer and oligomer. When either Chl a or Chl b was selectively excited, the observed decrease in Chl a fluorescence in the oligomer is proved to be caused mainly by the fast fluorescence quenching among Chl a molecules, rather than by the decrease in Chl b-to-Chl a singlet excitation transfer efficiency. Analyses of the picosecond time-resolved fluorescence kinetics identified two exponential de- cay components in all of the three forms of LHC II: a longer-lived component (4.1―4.7 ns) originating from fluorescence emission of Chl a, and a shorter-lived one (135―540 ps) from the rapid equilibration of singlet excitation among Chl a molecules. The time constant of excitation equilibration is 135 ps in oli- gomer, 520 ps in trimer and 540 ps in monomer. These results imply that LHC II in oligomer form is inherently able to quench Chl a excitation, a mecha- nism which may be related to the photoprotection of PS II via changing the degree of LHC II aggregation in Bryopsis corticulans.

Steady-state and time-resolved fluorescence spectroscopies have been used to study the excited state properties of Chl a in different aggregation forms of light-harvesting complex Ⅱ （LHC Ⅱ） from an intertidal green alga, Bryopsis corticulans, i.e. LHC Ⅱ monomer, trimer and oligomer. When either Chl a or Chl b was selectively excited, the observed decrease in Chl a fluorescence in the oligomer is proved to be caused mainly by the fast fluorescence quenching among Chl a molecules, rather than by the decrease in Chl b-to-Chl a singlet excitation transfer efficiency. Analyses of the picosecond time-resolved fluorescence kinetics identified two exponential decay components in all of the three forms of LHC Ⅱ： a longer-lived component （4.1 -4.7 ns） originating from fluorescence emission of Chl a, and a shorter-lived one （135-540 ps） from the rapid equilibration of singlet excitation among Chl a molecules. The time constant of excitation equilibration is 135 ps in oligomer, 520 ps in trimer and 540 ps in monomer. These results imply that LHC Ⅱ in oligomer form is inherently able to quench Chl a excitation, a mechanism which may be related to the photoprotection of PS Ⅱ via changing the degree of LHC Ⅱ aggregation in Bryopsis corticulans.