The role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll proteins

M.D. Wahadoszamen, I. Margalit, A.M. Ara, R. van Grondelle, D. Noy

Research output: Contribution to JournalArticleAcademicpeer-review


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.
Original languageEnglish
Article number5287
JournalNature Communications
Publication statusPublished - 2014


Bibliographical note

PT: J; NR: 33; TC: 0; J9: NAT COMMUN; PG: 8; GA: AS1SI; UT: WOS:000344060900001

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