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

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.

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

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.