title: Excitation decay pathways of Lhca proteins: a time-resolved fluorescence study.
abstract: Light-harvesting complex I (LHCI), which serves as a peripheral antenna for photosystem I (PSI) in green plants, consists mainly of four polypeptides, Lhca1-4. We report room temperature emission properties of individual reconstituted monomeric Lhca proteins (Lhca1, -2, -3, and -4) and dimeric Lhca1/4, performed by steady-state and time-resolved fluorescence techniques. The emission quantum yields of the samples are approximately 0.12, 0.085, 0.081, 0.041, and 0.063 for Lhca1, -2, -3, -4, and the -1/4 dimer, respectively, which is considerably lower than the value of 0.22 found for light-harvesting complex II (LHCII), the main peripheral antenna complex of photosystem II in green plants. The decay components of LHCI proteins can be divided in two categories: Lhca1 and Lhca3 have decay times of 1.1-1.6 ns and 3.3-3.6 ns, and Lhca2 and Lhca4 have decay times of 0.7-0.9 ns and 3.1-3.2 ns. These categories seem to correlate with the pigment composition of the samples. All decay times are faster than that observed previously for LHCII. When the absolute emission yields and the lifetimes of the Lhca samples are combined, the overall emission properties of the individual Lhca proteins are expressed in terms of their emitting dipole moment strength. In the samples without extreme red states, that is, Lhca1 and Lhca2, the emitting dipole moment has a value close to unity (relative to monomeric chlorophyll in acetone), which is similar to that for LHCII, whereas, in the samples with the red-most state (F-730), that is, Lhca3, -4, and the -1/4 dimer, the emitting dipole moment has a value less than unity (0.6-0.8), which can be explained by mixing the red-most (exciton) state with a dark charge-transfer state, as suggested in previous PSI red pigment studies. In addition, we find a lifetime component of approximately 50-150 ps in all red-pigment-containing samples, which cannot be due to "slow" energy transfer, but is instead assigned to an unrelaxed state of the pigment-protein, which, on this time-scale, is converted into the final emitting state.
authors.affiliation: Faculty of Sciences, Department of Physics and Astronomy, Vrije Universiteit, De Boelelaan 1081, 1081 HV Amsterdam, The Netherlands. janihal@nat.vu.nl
authors.forename: Janne A
authors.initials: JA
authors.lastname: Ihalainen
authors.forename: Roberta
authors.initials: R
authors.lastname: Croce
authors.forename: Tomas
authors.initials: T
authors.lastname: Morosinotto
authors.forename: Ivo H M
authors.initials: IH
authors.lastname: van Stokkum
authors.forename: Roberto
authors.initials: R
authors.lastname: Bassi
authors.forename: Jan P
authors.initials: JP
authors.lastname: Dekker
authors.forename: Rienk
authors.initials: R
authors.lastname: van Grondelle
mesh_terms: D029681:Arabidopsis Proteins; D061146:Chlorophyll Binding Proteins; D004735:Energy Transfer; D006207:Half-Life; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry*; D045331:Photosystem I Protein Complex / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*
chemical_list: D029681:Arabidopsis Proteins; D061146:Chlorophyll Binding Proteins; C490278:LHCA1 protein, Arabidopsis; C490277:Lhca2 protein, Arabidopsis; D045342:Light-Harvesting Protein Complexes; D045331:Photosystem I Protein Complex; D010940:Plant Proteins