title: Organization of bacteriochlorophylls in individual chlorosomes from Chlorobaculum tepidum studied by 2-dimensional polarization fluorescence microscopy.
abstract: Chlorosomes are the largest and most efficient natural light-harvesting systems and contain supramolecular assemblies of bacteriochlorophylls that are organized without proteins. Despite a recent structure determination for chlorosomes from Chlorobaculum tepidum (Ganapathy Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 8525), the issue of a possible large structural disorder is still discussed controversially. We have studied individual chlorosomes prepared under very carefully controlled growth condition by a novel 2-dimensional polarization single molecule imaging technique giving polarization information for both fluorescence excitation and emission simultaneously. Contrary to the existing literature data, the polarization degree or modulation depth (M) for both excitation (absorption) and emission (fluorescence) showed extremely narrow distributions. The fluorescence was always highly polarized with M ≈ 0.77, independent of the excitation wavelength. Moreover, the fluorescence spectra of individual chlorosomes were identical within the error limits. These results lead us to conclude that all chlorosomes possess the same type of internal organization in terms of the arrangement of the bacteriochlorophyll c transition dipole moments and their total excitonic transition dipole possess a cylindrical symmetry in agreement with the previously suggested concentric multitubular chlorophyll aggregate organization (Ganapathy Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 8525).
authors.affiliation: Chemical Physics, Lund University, Lund, Sweden.
authors.forename: Yuxi
authors.initials: Y
authors.lastname: Tian
authors.forename: Rafael
authors.initials: R
authors.lastname: Camacho
authors.forename: Daniel
authors.initials: D
authors.lastname: Thomsson
authors.forename: Michael
authors.initials: M
authors.lastname: Reus
authors.forename: Alfred R
authors.initials: AR
authors.lastname: Holzwarth
authors.forename: Ivan G
authors.initials: IG
authors.lastname: Scheblykin
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D001429:Bacteriochlorophylls / Q000737:chemistry*; D019414:Chlorobi / Q000737:chemistry*; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry*; D008856:Microscopy, Fluorescence
chemical_list: D001426:Bacterial Proteins; D001429:Bacteriochlorophylls; C086320:FMO bacteriochlorophyll protein, Bacteria; D045342:Light-Harvesting Protein Complexes