Observation of the energy-level structure of the low-light adapted B800 LH4 complex by single-molecule spectroscopy.
Low-light adapted B800 light-harvesting complex 4 (LH4) from Rhodopseudomonas palustris is a complex in which the arrangement of the bacteriochloropyll a pigments is very different from the well-known B800-850 LH2 complex. For bulk samples, the main spectroscopic feature in the near-infrared is the occurrence of a single absorption band at 802 nm. Single-molecule spectroscopy can resolve the narrow bands that are associated with the exciton states of the individual complexes. The low temperature (1.2 K) fluorescence excitation spectra of individual LH4 complexes are very heterogeneous and display unique features. It is shown that an exciton model can adequately reproduce the polarization behavior of the complex, the experimental distributions of the number of observed peaks per complex, and the widths of the absorption bands. The results indicate that the excited states are mainly localized on one or a few subunits of the complex and provide further evidence supporting the recently proposed structure model.
de Ruijter
W P F
WP
Department of Biophysics, Leiden University, Leiden, The Netherlands.
Oellerich
S
S
Segura
J-M
JM
Lawless
A M
AM
Papiz
M
M
Aartsma
T J
TJ
D000465:Algorithms; D001426:Bacterial Proteins / Q000737:chemistry*; D003198:Computer Simulation; D004307:Dose-Response Relationship, Radiation; D004735:Energy Transfer / Q000528:radiation effects*; D008027:Light; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry* / Q000528:radiation effects*; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation / Q000528:radiation effects; D013055:Spectrophotometry, Infrared / Q000379:methods*
D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes