Chirality-based signatures of local protein environments in two-dimensional optical spectroscopy of two species photosynthetic complexes of green sulfur bacteria: simulation study.
Two-dimensional electronic chirality-induced signals of excitons in the photosynthetic Fenna-Matthews-Olson complex from two species of green sulfur bacteria (Chlorobium tepidum and Prosthecochloris aestuarii) are compared. The spectra are predicted to provide sensitive probes of local protein environment of the constituent bacteriochlorophyll a chromophores and reflect electronic structure variations (site energies and couplings) of the two complexes. Pulse polarization configurations are designed that can separate the coherent and incoherent exciton dynamics contributions to the two-dimensional spectra.
Voronine
Dmitri V
DV
Department of Chemistry, University of California, Irvine, California 92697-2025, USA.
Abramavicius
Darius
D
Mukamel
Shaul
S
D001426:Bacterial Proteins / Q000737:chemistry* / Q000528:radiation effects / Q000648:ultrastructure*; D019414:Chlorobi / Q000737:chemistry* / Q000528:radiation effects*; D003198:Computer Simulation; D008027:Light; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry* / Q000528:radiation effects / Q000648:ultrastructure*; D008954:Models, Biological; D008956:Models, Chemical; D008958:Models, Molecular; D013045:Species Specificity; D013057:Spectrum Analysis / Q000379:methods; D013237:Stereoisomerism
D001426:Bacterial Proteins; C086320:FMO bacteriochlorophyll protein, Bacteria; D045342:Light-Harvesting Protein Complexes