Band structure and local dynamics of excitons in bacterial light-harvesting complexes revealed by spectrally selective spectroscopy.
Hole-burned absorption and line-narrowed fluorescence spectra are studied at 5 K in wild type and mutant LH1 and LH2 antenna preparations from the photosynthetic purple bacterium Rhodobacter sphaeroides. Evidence was found in all samples, even in intact membranes, of the presence of a broad distribution of bacteriochlorophyll species that are unable to communicate energy between each other and to the exciton states of functional antenna complexes. The distribution maximum of these localized species determined by zero phonon hole action spectroscopy is at 783.5 nm in purified LH1 complexes and at 786.8 nm in B850-only mutant LH2 complexes. A well-resolved peak at 807 nm in LH1 complexes is assigned to the exciton band structure of functional core antenna complexes. Similar structure in LH2 complexes overlaps with the distribution of localized species. Off-diagonal (structural) disorder may be responsible for this exciton band structure. Our data also imply that pair-wise inter-chlorophyll couplings determine the resonance fluorescence lineshape of excitonic polarons.
Rätsep
Margus
M
Institute of Physics, University of Tartu, Riia 142, Tartu, 51014, Estonia.
Hunter
C Neil
CN
Olsen
John D
JD
Freiberg
Arvi
A
D045342:Light-Harvesting Protein Complexes / Q000737:chemistry* / Q000235:genetics; D009154:Mutation / Q000235:genetics; D012242:Rhodobacter sphaeroides / Q000737:chemistry* / Q000235:genetics; D013057:Spectrum Analysis
D045342:Light-Harvesting Protein Complexes