title: Excitation energy transfer from phycobiliprotein to chlorophyll d in intact cells of Acaryochloris marina studied by time- and wavelength-resolved fluorescence spectroscopy.
abstract: The fluorescence decay spectra and the excitation energy transfer from the phycobiliproteins (PBP) to the chlorophyll-antennae of intact cells of the chlorophyll (Chl) d-dominated cyanobacterium Acaryochloris marina were investigated at 298 and 77 K by time- and wavelength-correlated single photon counting fluorescence spectroscopy. At 298 K it was found that (i) the fluorescence dynamics in A. marina is characterized by two emission peaks located at about 650 and 725 nm, (ii) the intensity of the 650 nm fluorescence depends strongly on the excitation wavelength, being high upon excitation of phycobiliprotein (PBP) at 632 nm but virtually absent upon excitation of chlorophyll at 430 nm, (iii) the 650 nm fluorescence band decayed predominantly with a lifetime of 70 +/- 20 ps, (iv) the 725 nm fluorescence, which was observed independent of the excitation wavelength, can be described by a three-exponential decay kinetics with lifetimes depending on the open or the closed state (F(0) or F(m)) of the reaction centre of Photosystem II (PS II). Based on the results of this study, it is inferred that the excitation energy transfer from phycobiliproteins to Chl d of PS II in A. marina occurs with a time constant of about 70 ps, which is about three times faster than the energy transfer from the phycobilisomes to PS II in the Chl a-containing cyanobacterium Synechococcus 6301. A similar fast PBP to Chl d excitation energy transfer was also observed at 77 K. At 77 K a small long-lived fluorescence decay component with a lifetime of 14 ns was observed in the 640-700 nm spectral range. However, it has a rather featureless spectrum, not typical for Chl a, and was only observed upon excitation at 400 nm but not upon excitation at 632 and 654 nm. Thus, this long-lived fluorescence component cannot be used as an indicator that the primary PS II donor of Acaryochloris marina contains Chl a.
authors.affiliation: Institute of Optics, Technical University Berlin, Germany.
authors.forename: Zdenek
authors.initials: Z
authors.lastname: Petrásek
authors.forename: Franz-Josef
authors.initials: FJ
authors.lastname: Schmitt
authors.forename: Christoph
authors.initials: C
authors.lastname: Theiss
authors.forename: Joachim
authors.initials: J
authors.lastname: Huyer
authors.forename: Min
authors.initials: M
authors.lastname: Chen
authors.forename: Anthony
authors.initials: A
authors.lastname: Larkum
authors.forename: Hans Joachim
authors.initials: HJ
authors.lastname: Eichler
authors.forename: Klaus
authors.initials: K
authors.lastname: Kemnitz
authors.forename: Hann-Jörg
authors.initials: HJ
authors.lastname: Eckert
mesh_terms: D002734:Chlorophyll / Q000737:chemistry / Q000378:metabolism*; D000458:Cyanobacteria / Q000166:cytology* / Q000378:metabolism*; D004735:Energy Transfer; D007700:Kinetics; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013696:Temperature; D013997:Time Factors
chemical_list: D045342:Light-Harvesting Protein Complexes; D002734:Chlorophyll; C107509:chlorophyll d