Impact of Single-Point Mutations on the Excitonic Structure and Dynamics in a Fenna–Matthews–Olson Complex

Khmelnitskiy, Anton; Reinot, T.; Jankowiak, Ryszard

doi:10.1021/acs.jpclett.8b01396

Cited by 11 publications

(15 citation statements)

References 41 publications

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“…In summary, our results show that the excitonic structure and dynamics of the FMO complex are very sensitive to the local environment around BChl 6. Even a small change, such as a single-point mutation near BChl 6, can cause changes in several exciton states, resulting in a noticeable change in the absorption 31 and Khmelnitskiy et al 33 showed that most of the mutant spectra exhibited some degree of changes, but only the W184F mutant (near BChl 6) resulted in amplitude reversion of the 806 nm and 815 nm bands, which is consistent with our results. This is due to the position and orientation of BChl 6 in the FMO complex that enables strong couplings with its nearby BChls 5 and 7.…”

Section: ■ Results and Discussionsupporting

confidence: 93%

Theoretical Study of the Spectral Differences of the Fenna–Matthews–Olson Protein from Different Species and Their Mutants

Huai

Tong

et al. 2021

J. Phys. Chem. B

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The structural basis for the spectral differences between the Fenna–Matthews–Olson (FMO) proteins from Chlorobaculum tepidum (C. tepidum) and Prosthecochloris aestuarii 2K (P. aestuarii) is yet to be fully understood. Mutation-induced perturbation to the exciton structure and the optical spectra of the complex provide a suitable means to investigate the critical role played by the protein scaffold. In this work, we have performed quantum-mechanics/molecular-mechanics calculations over the molecular dynamics simulation trajectories with the polarized protein-specific charge scheme for both wild-type FMOs and two mutants. Our result reveals that a single-point mutation in the vicinity of BChl 6, namely, W183F of C. tepidum, significantly affects the absorption spectrum, resulting in a switch of the absorption spectrum from type 2, for which the 806 nm band is more pronounced than the 815 nm band, to type 1, for which the 815 nm band is pronounced. Our observations agree with the single-point mutation experiments reported by Saer et al. (Biochim. Biophys. Acta, Bioenerg. 2017, 1858, 288–296) and Khmelnitskiy et al. (J. Phys. Chem. Lett. 2018, 9, 3378–3386). In contrast, the absorption spectrum of the P. aestuarii experiences the opposite transition (from type 1 to type 2) upon the same mutation. Furthermore, by comparing the contributions of individual pigments to the spectra in the wild type and its mutant, we find that a single-point mutation near BChl 6 not only induces changes in excitation energy of BChl 6 per se but also affects the excitonic structures of the neighboring BChls 5 and 7 through strong interpigment electronic couplings, resulting in a significant change in the absorption spectra.

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Section: ■ Results and Discussionsupporting

confidence: 93%

Theoretical Study of the Spectral Differences of the Fenna–Matthews–Olson Protein from Different Species and Their Mutants

Huai

Tong

et al. 2021

J. Phys. Chem. B

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“…Populations determined by generalized Förster rates calculated according to §3. Adapted from [66]. (Online version in colour.…”

Section: Discussionmentioning

confidence: 99%

“…In this case, the trimeric organization with the same SDF for each BChl 3 leads to a triple splitting of the 825 nm absorption band. Adapted from[66]. (Online version in colour.)…”

mentioning

confidence: 99%

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

Kell

Khmelnitskiy

Reinot

et al. 2019

J. R. Soc. Interface.

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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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“…The Fenna–Matthews–Olson (FMO) pigment–protein complex, found in green sulfur bacteria, is one of the most thoroughly studied photosynthetic proteins (see Figure ). − The primary function of FMO is to transfer the excitation energy from a much larger chlorosome antenna to the intramembrane reaction center complex, where electronic excitation initiates charge transfer process.…”

mentioning

confidence: 99%

Predictive First-Principles Modeling of a Photosynthetic Antenna Protein: The Fenna–Matthews–Olson Complex

Kim

Morozov

Stadnytskyi

et al. 2020

J. Phys. Chem. Lett.

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Impact of Single-Point Mutations on the Excitonic Structure and Dynamics in a Fenna–Matthews–Olson Complex

Cited by 11 publications

References 41 publications

Theoretical Study of the Spectral Differences of the Fenna–Matthews–Olson Protein from Different Species and Their Mutants

Theoretical Study of the Spectral Differences of the Fenna–Matthews–Olson Protein from Different Species and Their Mutants

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

Predictive First-Principles Modeling of a Photosynthetic Antenna Protein: The Fenna–Matthews–Olson Complex

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