title: Time-Resolved fluorescence studies on the internal motion of chlorophyll a of light-harvesting chlorophyll a/b-protein complex in lipid membranes.
abstract: By analyzing the steady state and time-resolved fluorescence anisotropy, the internal motions of chlorophyll a of light-harvesting chlorophyll a/b-protein complex (LHCII) were characterized in a dimyristoylphosphatidylcholine (DMPC) liposome. Corresponding to the thermotropic phase of the membrane, chlorophyll a showed an unique internal motion in LHCII. At the gel phase, two motional components, one fast and the other slow, were observed, which would originate in the heterogeneity of the mutual orientation and the binding site of the chlorophyll a in LHCII. Interestingly, the faster motion was suppressed and only the slower segmental rotation with the larger motional amplitude was allowed on the phase transition to a liquid crystalline phase.
authors.affiliation: Structural Biophysics Laboratory, RIKEN Harima Institute, Hyogo, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Furuichi
authors.forename: E
authors.initials: E
authors.lastname: Nishimoto
authors.forename: T
authors.initials: T
authors.lastname: Koga
authors.forename: S
authors.initials: S
authors.lastname: Yamashita
mesh_terms: D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002734:Chlorophyll / Q000737:chemistry*; D000077194:Chlorophyll A; D004134:Dimyristoylphosphatidylcholine; D005454:Fluorescence Polarization; D045342:Light-Harvesting Protein Complexes; D008081:Liposomes; D008112:Liver Glycogen / Q000737:chemistry; D008563:Membrane Lipids / Q000737:chemistry*; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D011817:Rabbits; D013696:Temperature
chemical_list: D045342:Light-Harvesting Protein Complexes; D008081:Liposomes; D008112:Liver Glycogen; D008563:Membrane Lipids; D045322:Photosynthetic Reaction Center Complex Proteins; D002734:Chlorophyll; D004134:Dimyristoylphosphatidylcholine; D000077194:Chlorophyll A