6533b7d4fe1ef96bd126282b

RESEARCH PRODUCT

Ultrafast excitation dynamics of low energy pigments in reconstituted peripheral light-harvesting complexes of photosystem I

Harald PaulsenAlexander N. MelkozernovRobert E. BlankenshipGregory W. SchmidtVolkmar H.r. SchmidSu Lin

subject

Time-resolved spectroscopyPhotosystem I0106 biological sciencesAbsorption spectroscopyPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiophysicsPhotochemistryPhotosystem I01 natural sciences7. Clean energyBiochemistryFluorescence spectroscopyLight-harvesting complexExcitation energy transfer03 medical and health scienceschemistry.chemical_compoundStructural BiologyUltrafast laser spectroscopyGeneticsMolecular BiologyPlant Proteins030304 developmental biology0303 health sciencesPhotosystem I Protein ComplexSpectrophotometry AtomicPigments BiologicalCell BiologyPlantsLHCI-730 heterodimerEnergy TransferchemistryAntennaChlorophyllPicosecondChlorophyll Binding ProteinsLight-harvesting complexTime-resolved spectroscopyDimerization010606 plant biology & botany

description

AbstractUltrafast dynamics of a reconstituted Lhca4 subunit from the peripheral LHCI-730 antenna of photosystem I of higher plants were probed by femtosecond absorption spectroscopy at 77 K. Intramonomeric energy transfer from chlorophyll (Chl) b to Chl a and energy equilibration between Chl a molecules observed on the subpicosecond time scale are largely similar to subpicosecond energy equilibration processes within LHCII monomers. However, a 5 ps equilibration process in Lhca4 involves unique low energy Chls in LHCI absorbing at 705 nm. These pigments localize the excitation both in the Lhca4 subunit and in LHCI-730 heterodimers. An additional 30–50 ps equilibration process involving red pigments of Lhca4 in the heterodimer, observed by transient absorption and picosecond fluorescence spectroscopy, was ascribed to intersubunit energy transfer.

https://doi.org/10.1016/s0014-5793(00)01370-3