Energy transfer from carotenoid and FMO-protein in subcellular preparations from green sulfur bacteria. Spectroscopic characterization of an FMO-reaction center core complex at low temperature

1996 ◽  
Vol 50 (1) ◽  
pp. 71-77 ◽  
Author(s):  
Christof Francke ◽  
Stephan C. M. Otte ◽  
Mette Miller ◽  
Jan Amesz ◽  
John M. Olson
Keyword(s):  
Energy Transfer ◽  
Low Temperature ◽  
Reaction Center ◽  
Spectroscopic Characterization ◽  
Green Sulfur Bacteria ◽  
Core Complex ◽  
Sulfur Bacteria ◽  
Fmo Protein ◽  
Green Sulfur

scholarly journals On uncorrelated inter-monomer Förster energy transfer in Fenna–Matthews–Olson complexes

2019 ◽  
Vol 16 (151) ◽  
pp. 20180882 ◽  
Author(s):  
Adam Kell ◽  
Anton Yu. Khmelnitskiy ◽  
Tonu Reinot ◽  
Ryszard Jankowiak
Keyword(s):  
Energy Transfer ◽  
Green Sulfur Bacteria ◽  
Coupling Constants ◽  
Electronic Coupling ◽  
Reaction Centre ◽  
Sulfur Bacteria ◽  
Fmo Protein ◽  
Reduced Density ◽  
Light Harvesting Antenna ◽  
Pigment Protein Complex

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 considering only sub-picosecond time scales or assuming that the inter-monomer coupling between low-energy states is too weak to warrant consideration of the entire trimer. However, Förster theory predicts that energy transfer of the order of picoseconds is possible even for very weak (less than 5 cm –1 ) electronic coupling between chromophores. This work reviews experimental data (with a focus on emission and hole-burned spectra) and simulations of exciton dynamics which demonstrate inter-monomer energy transfer. It is shown that the lowest energy 825 nm absorbance band cannot be properly described by a single excitonic state. The energy transfer through FMO is modelled by generalized Förster theory using a non-Markovian, reduced density matrix approach to describe the electronic structure. The disorder-averaged inter-monomer transfer time across the 825 nm band is about 27 ps. While only isolated FMO proteins are presented, the presence of inter-monomer energy transfer in the context of the overall photosystem is also briefly discussed.

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