Dynamics of Energy and Electron Transfer in the FMO-Reaction Center Core Complex from the Phototrophic Green Sulfur Bacterium <i>Chlorobaculum tepidum</i>

He, Guannan; Niedzwiedzki, Dariusz M.; Orf, Gregory S.; Zhang, Hao; Blankenship, Robert E.

doi:10.1021/acs.jpcb.5b04170

Cited by 33 publications

(45 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, transient absorption measurements on an FMO/RCC system could not definitively assign an FMO ! RC transfer time owing to spectral overlap of BChls bound to each protein and an inherent inability to initially excite only FMO [73]. Thus, future work is needed to further investigate energy transfer to the RC.…”

Section: Rate Equationsmentioning

confidence: 99%

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

Kell

Khmelnitskiy

Reinot

et al. 2019

J. R. Soc. Interface.

View full text Add to dashboard Cite

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.

show abstract

Section: Rate Equationsmentioning

confidence: 99%

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

Kell

Khmelnitskiy

Reinot

et al. 2019

J. R. Soc. Interface.

View full text Add to dashboard Cite

show abstract

“…). Energy absorbed by the FMO is (at least partially) transferred to the RCs , and hence contributes to the broad emission of the RC with its maximum at 842 nm.…”

Section: Resultsmentioning

confidence: 99%

Origin of bimodal fluorescence enhancement factors of Chlorobaculum tepidum reaction centers on silver island films

et al. 2016

View full text Add to dashboard Cite

We focus on the spectral dependence of plasmon-induced enhancement of fluorescence of Chlorobaculum tepidum reaction centers. When deposited on silver island film, they exhibit up to a 60-fold increase in fluorescence. The dependence of enhancement factors on the excitation wavelength is not correlated with the absorption spectrum of the plasmonic structure. In particular, the presence of one (or multiple) trimers of the Fenna-Matthews-Olson (FMO) protein reveals itself in bimodal distribution of enhancement factors for the excitation at 589 nm, the wavelength corresponding to bacteriochlorophyll absorption of FMO and the core of the RC. We conclude that the structure of multichromophoric complexes can substantially affect the impact of plasmonic excitations, which is important in the context of assembling functional biohybrid systems.

show abstract

“…The reaction center (RC) from Chlorobaculum (C.) tepidum is an example of a much larger complex, as compared to PCP, although its detailed structure is not known at present. It contains bacteriochlorophyll a (BChl a), Chls a, and carotenoid molecules [35][36][37][38][39][40]. The contribution of each type of pigment is visible in the absorption spectrum ( Figure 2d).…”

Section: Photosynthetic Complexesmentioning

confidence: 99%

Silver Island Film for Enhancing Light Harvesting in Natural Photosynthetic Proteins

Kowalska

Szalkowski

Sulowska

et al. 2020

IJMS

View full text Add to dashboard Cite

The effects of combining naturally evolved photosynthetic pigment–protein complexes with inorganic functional materials, especially plasmonically active metallic nanostructures, have been a widely studied topic in the last few decades. Besides other applications, it seems to be reasonable using such hybrid systems for designing future biomimetic solar cells. In this paper, we describe selected results that point out to various aspects of the interactions between photosynthetic complexes and plasmonic excitations in Silver Island Films (SIFs). In addition to simple light-harvesting complexes, like peridinin-chlorophyll-protein (PCP) or the Fenna–Matthews–Olson (FMO) complex, we also discuss the properties of large, photosynthetic reaction centers (RCs) and Photosystem I (PSI)—both prokaryotic PSI core complexes and eukaryotic PSI supercomplexes with attached antenna clusters (PSI-LHCI)—deposited on SIF substrates.

show abstract

Dynamics of Energy and Electron Transfer in the FMO-Reaction Center Core Complex from the Phototrophic Green Sulfur Bacterium Chlorobaculum tepidum

Cited by 33 publications

References 44 publications

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

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

Origin of bimodal fluorescence enhancement factors of Chlorobaculum tepidum reaction centers on silver island films

Silver Island Film for Enhancing Light Harvesting in Natural Photosynthetic Proteins

Contact Info

Product

Resources

About