fmo protein
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2019 ◽  
Vol 16 (151) ◽  
pp. 20180882 ◽  
Author(s):  
Adam Kell ◽  
Anton Yu. Khmelnitskiy ◽  
Tonu Reinot ◽  
Ryszard Jankowiak

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.


2016 ◽  
Vol 113 (31) ◽  
pp. E4486-E4493 ◽  
Author(s):  
Gregory S. Orf ◽  
Rafael G. Saer ◽  
Dariusz M. Niedzwiedzki ◽  
Hao Zhang ◽  
Chelsea L. McIntosh ◽  
...  

Light-harvesting antenna complexes not only aid in the capture of solar energy for photosynthesis, but regulate the quantity of transferred energy as well. Light-harvesting regulation is important for protecting reaction center complexes from overexcitation, generation of reactive oxygen species, and metabolic overload. Usually, this regulation is controlled by the association of light-harvesting antennas with accessory quenchers such as carotenoids. One antenna complex, the Fenna–Matthews–Olson (FMO) antenna protein from green sulfur bacteria, completely lacks carotenoids and other known accessory quenchers. Nonetheless, the FMO protein is able to quench energy transfer in aerobic conditions effectively, indicating a previously unidentified type of regulatory mechanism. Through de novo sequencing MS, chemical modification, and mutagenesis, we have pinpointed the source of the quenching action to cysteine residues (Cys49 and Cys353) situated near two low-energy bacteriochlorophylls in the FMO protein from Chlorobaculum tepidum. Removal of these cysteines (particularly removal of the completely conserved Cys353) through N-ethylmaleimide modification or mutagenesis to alanine abolishes the aerobic quenching effect. Electrochemical analysis and electron paramagnetic resonance spectra suggest that in aerobic conditions the cysteine thiols are converted to thiyl radicals which then are capable of quenching bacteriochlorophyll excited states through electron transfer photochemistry. This simple mechanism has implications for the design of bio-inspired light-harvesting antennas and the redesign of natural photosynthetic systems.


2014 ◽  
Vol 119 (21) ◽  
pp. 5197-5206 ◽  
Author(s):  
Oliviero Andreussi ◽  
Stefano Caprasecca ◽  
Lorenzo Cupellini ◽  
Ingrid Guarnetti-Prandi ◽  
Ciro A. Guido ◽  
...  

2014 ◽  
Vol 5 (8) ◽  
pp. 1450-1456 ◽  
Author(s):  
Adam Kell ◽  
Khem Acharya ◽  
Valter Zazubovich ◽  
Ryszard Jankowiak

2010 ◽  
Vol 2 (2) ◽  
pp. 93-98 ◽  
Author(s):  
Marcel Schmidt am Busch ◽  
Frank Müh ◽  
Mohamed El-Amine Madjet ◽  
Thomas Renger

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