98 research outputs found
Conformational relaxation following reduction of the photoactive bacteriopheophytin in reaction centers from Blastochloris viridis. Influence of mutations at position M208
AbstractThe photochemically trapped bacteriopheophytin (BPh) b radical anion in the active branch (ΦA−) of reaction centers (RCs) from Blastochloris (formerly called Rhodopseudomonas) viridis is characterized by 1H-ENDOR as well as optical absorption spectroscopy. The two site-directed mutants YF(M208) and YL(M208), in which tyrosine at position M208 is replaced by phenylalanine and leucine, respectively, are investigated and compared with the wild type. The residue at M208 is in close proximity to the primary electron donor, P, the monomeric bacteriochlorophyll (BChl), BA, and the BPh, ΦA, that are involved in the transmembrane electron transfer to the quinone, QA, in the RC. The analysis of the ENDOR spectra of ΦA− at 160 K indicates that two distinct states of ΦA− are present in the wild type and the mutant YF(M208). Based on a comparison with ΦA− in RCs of Rhodobacter sphaeroides the two states are interpreted as torsional isomers of the 3-acetyl group of ΦA. Only one ΦA− state occurs in the mutant YL(M208). This effect of the leucine residue at position M208 is explained by steric hindrance that locks the acetyl group in one specific position. On the basis of these results, an interpretation of the optical absorption difference spectrum of the state ΦA−QA− is attempted. This state can be accumulated at 100 K and undergoes an irreversible change between 100 and 200 K [Tiede et al., Biochim. Biophys. Acta 892 (1987) 294–302]. The corresponding absorbance changes in the BChl Qx and Qy regions observed in the wild type also occur in the YF(M208) mutant but not in YL(M208). The observed changes in the wild type and YF(M208) are assigned to RCs in which the 3-acetyl group of ΦA changes its orientation. It is concluded that this distinct structural relaxation of ΦA can significantly affect the optical properties of BA and contribute to the light-induced absorption difference spectra
Suppression of quantum oscillations and the dependence on site energies in electronic excitation transfer in the Fenna-Matthews-Olson trimer
Energy transfer in the photosynthetic complex of the Green Sulfur Bacteria
known as the Fenna-Matthews-Olson (FMO) complex is studied theoretically taking
all three subunits (monomers) of the FMO trimer and the recently found eighth
bacteriochlorophyll (BChl) molecule into account. We find that in all
considered cases there is very little transfer between the monomers. Since it
is believed that the eighth BChl is located near the main light harvesting
antenna we look at the differences in transfer between the situation when BChl
8 is initially excited and the usually considered case when BChl 1 or 6 is
initially excited. We find strong differences in the transfer dynamics, both
qualitatively and quantitatively. When the excited state dynamics is
initialized at site eight of the FMO complex, we see a slow exponential-like
decay of the excitation. This is in contrast to the oscillations and a
relatively fast transfer that occurs when only seven sites or initialization at
sites 1 and 6 is considered. Additionally we show that differences in the
values of the electronic transition energies found in the literature lead to a
large difference in the transfer dynamics
Role of quantum coherence in chromophoric energy transport
The role of quantum coherence and the environment in the dynamics of
excitation energy transfer is not fully understood. In this work, we introduce
the concept of dynamical contributions of various physical processes to the
energy transfer efficiency. We develop two complementary approaches, based on a
Green's function method and energy transfer susceptibilities, and quantify the
importance of the Hamiltonian evolution, phonon-induced decoherence, and
spatial relaxation pathways. We investigate the Fenna-Matthews-Olson protein
complex, where we find a contribution of coherent dynamics of about 10% and of
relaxation of 80%.Comment: 5 pages, 3 figures, included static disorder, correlated environmen
Challenges facing an understanding of the nature of low-energy excited states in photosynthesis
© 2016 Elsevier B.V. While the majority of the photochemical states and pathways related to the biological capture of solar energy are now well understood and provide paradigms for artificial device design, additional low-energy states have been discovered in many systems with obscure origins and significance. However, as low-energy states are naively expected to be critical to function, these observations pose important challenges. A review of known properties of low energy states covering eight photochemical systems, and options for their interpretation, are presented. A concerted experimental and theoretical research strategy is suggested and outlined, this being aimed at providing a fully comprehensive understanding
Revisiting the optical properties of the FMO protein
We review the optical properties of the FMO complex as found by spectroscopic studies of the Qy band over the last two decades. This article emphasizes the different methods used, both experimental and theoretical, to elucidate the excitonic structure and dynamics of this pigment–protein complex
EPR, ENDOR, and Special TRIPLE measurements of P•+ in wild type and modified reaction centers from Rb. sphaeroides
Mössbauer Spectroscopy on Respiratory Complex I: The Iron–Sulfur Cluster Ensemble in the NADH-Reduced Enzyme Is Partially Oxidized
Scalable High-Performance Algorithm for the Simulation of Exciton Dynamics. Application to the Light-Harvesting Complex II in the Presence of Resonant Vibrational Modes
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