title: B800-B850 coherence correlates with energy transfer rates in the LH2 complex of photosynthetic purple bacteria.
abstract: Until recently, no analytical measure of many-body delocalization in open systems had been developed, yet such a measure enables characterization of how molecular excitons delocalize in photosynthetic light-harvesting complexes, and in turn helps us understand quantum coherent aspects of electronic energy transfer. In this paper we apply these measures to a model peripheral light-harvesting complex, LH2 from Rhodopseudomonas acidophila. We find how many chromophores collectively contribute to the "delocalization length" of an excitation within LH2 and how the coherent delocalization is distributed spatially. We also investigate to what extent this delocalization length is effective, by examining the impact of bipartite and multipartite entanglement in inter-ring energy transfer in LH2.
authors: Department of Physics, University of Toronto, Toronto, Canada.
authors: Cathal
authors: C
authors: Smyth
authors: Department of Chemistry, Princeton University, Washington Rd, Princeton, NJ 08544, USA. gscholes@princeton.edu.
authors: Daniel G
authors: DG
authors: Oblinsky
authors: Department of Chemistry, Princeton University, Washington Rd, Princeton, NJ 08544, USA. gscholes@princeton.edu.
authors: Gregory D
authors: GD
authors: Scholes
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001429:Bacteriochlorophylls / Q000737:chemistry; D004735:Energy Transfer; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry / Q000378:metabolism*; D010788:Photosynthesis; D011789:Quantum Theory; D012241:Rhodopseudomonas / Q000378:metabolism*
chemical_list: C081521:B800-850 light-harvesting complex, bacteria; D001426:Bacterial Proteins; D001429:Bacteriochlorophylls; D045342:Light-Harvesting Protein Complexes