On uncorrelated inter-monomer Forster energy transfer in Fenna-Matthews-Olson complexes.

ABSTRACT: The Fenna-Matthews-Olson (FMO) light-harvesting antenna protein of green sulfur bacteria is a long-studied pigment-protein complex which funnels energy from the chlorosome to the reaction centre where photochemistry takes place. The structure of the FMO protein from Chlorobaculum tepidum is known as a homotrimeric complex containing eight bacteriochlorophyll a per monomer. Owing to this structure FMO has strong intra-monomer and weak inter-monomer electronic coupling constants. While long-lived (sub-picosecond) coherences within a monomer have been a prevalent topic of study over the past decade, various experimental evidence supports the presence of subsequent inter-monomer energy transfer on a picosecond time scale. The latter has been neglected by most authors in recent years by conside

SUBMITTER: Kell A 

PROVIDER: S-EPMC6408346 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature