title: The role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll proteins.
abstract: Understanding how specific protein environments affect the mechanisms of non-radiative energy dissipation within densely assembled chlorophylls in photosynthetic protein complexes is of great interest to the construction of bioinspired solar energy conversion devices. Mixing of charge-transfer and excitonic states in excitonically interacting chlorophylls was implicated in shortening excited states' lifetimes, but its relevance to active control of energy dissipation in natural systems is under considerable debate. Here we show that the degree of fluorescence quenching in two similar pairs of excitonically interacting bacteriochlorophyll derivatives is directly associated with increasing charge-transfer character in the excited state, and that the protein environment may control non-radiative dissipation by affecting the mixing of charge-transfer and excitonic states. The capability of local protein environments to determine the fate of excited states, and thereby to confer different functionalities to excitonically coupled dimers substantiates the dimer as the basic functional element of photosynthetic enzymes.
authors.affiliation: 1] Section of Biophysics, Department of Physics and Astronomy, VU University Amsterdam, Amsterdam 1081 HV, The Netherlands [2] Department of Physics, University of Dhaka, Dhaka 1000, Bangladesh.
authors.forename: Md
authors.initials: M
authors.lastname: Wahadoszamen
authors.affiliation: 1] Plant Sciences Department, Weizmann Institute of Science, Rehovot 7610001, Israel [2] Migal-Galilee Research Institute, Kiryat-Shmona 1101602, Israel.
authors.forename: Iris
authors.initials: I
authors.lastname: Margalit
authors.affiliation: 1] Section of Biophysics, Department of Physics and Astronomy, VU University Amsterdam, Amsterdam 1081 HV, The Netherlands [2] Department of Physics, Jagannath University, Dhaka 1100, Bangladesh.
authors.forename: Anjue Mane
authors.initials: AM
authors.lastname: Ara
authors.affiliation: Section of Biophysics, Department of Physics and Astronomy, VU University Amsterdam, Amsterdam 1081 HV, The Netherlands.
authors.forename: Rienk
authors.initials: R
authors.lastname: van Grondelle
authors.affiliation: Migal-Galilee Research Institute, Kiryat-Shmona 1101602, Israel.
authors.forename: Dror
authors.initials: D
authors.lastname: Noy
mesh_terms: D065966:Absorption, Physicochemical; D001426:Bacterial Proteins / Q000378:metabolism*; D001429:Bacteriochlorophylls / Q000378:metabolism*; D004583:Electrons; D004735:Energy Transfer; D050505:Mutant Proteins / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D015032:Zinc / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D001429:Bacteriochlorophylls; D050505:Mutant Proteins; D015032:Zinc