اشترك بالحزمة الذهبية واحصل على وصول غير محدود شمرا أكاديميا
تسجيل مستخدم جديدRole of Energy-Level Mismatches in a Multi-Pathway Complex of Photosynthesis
127
0
0.0
(
0
)
اسأل ChatGPT حول البحث
ﻻ يوجد ملخص باللغة العربية
Considering a multi-pathway structure in a light-harvesting complex of photosynthesis, we investigate the role of energy-level mismatches between antenna molecules in transferring the absorbed energy to a reaction center. We find a condition in which the antenna molecules faithfully play their roles: Their effective absorption ratios are larger than those of the receiver molecule directly coupled to the reaction center. In the absence of energy-level mismatches and dephasing noise, there arises quantum destructive interference between multiple paths that restricts the energy transfer. On the other hand, the destructive interference diminishes as asymmetrically biasing the energy-level mismatches and/or introducing quantum noise of dephasing for the antenna molecules, so that the transfer efficiency is greatly enhanced to near unity. Remarkably, the near-unity efficiency can be achieved at a wide range of asymmetric energy-level mismatches. Temporal characteristics are also optimized at the energy-level mismatches where the transfer efficiency is near unity. We discuss these effects, in particular, for the Fenna-Matthews-Olson complex.
قيم البحث
اقرأ أيضاً
Previous studies of the flexibilities of ancestral proteins suggests that proteins evolve their function by altering their native state ensemble. Here we propose a more direct method of visualizing this by measuring the changes in the vibrational den
sity of states (VDOS) of proteins as they evolve. Through analysis of VDOS profiles of ancestral and extant proteins we observe that $beta$-lactamase and thioredoxins evolve by altering their density of states in the terahertz region. Particularly, the shift in VDOS profiles between ancestral and extant proteins suggests that nature utilize dynamic allostery for functional evolution. Moreover, we also show that VDOS profile of individual position can be used to describe the flexibility changes, particularly those without any amino acid substitution.
Photosynthetic systems utilize adaptability to respond efficiently to fluctuations in their light environment. As a result, large photosynthetic yields can be achieved in conditions of low light intensity, while photoprotection mechanisms are activat
ed in conditions of elevated light intensity. In sharp contrast with these observations, current theoretical models predict bacterial cell death for physiologically high light intensities. To resolve this discrepancy, we consider a unified framework to describe three stages of photosynthesis in natural conditions, namely light absorption, exciton transfer and charge separation dynamics, to investigate the relationship between the statistical features of thermal light and the Quinol production in bacterial photosynthesis. This approach allows us to identify a mechanism of photoprotection that relies on charge recombination facilitated by the photon bunching statistics characteristic of thermal sunlight. Our results suggest that the flexible design underpinning natural photosynthesis may therefore rely on exploiting the temporal correlations of thermal light, manifested in photo-bunching patterns, which are preserved for excitations reaching the reaction center.
In multi-resolution simulations, different system components are simultaneously modelled at different levels of resolution, these being smoothly coupled together. In the case of enzyme systems, computationally expensive atomistic detail is needed in
the active site to capture the chemistry of substrate binding. Global properties of the rest of the protein also play an essential role, determining the structure and fluctuations of the binding site; however, these can be modelled on a coarser level. Similarly, in the most computationally efficient scheme only the solvent hydrating the active site requires atomistic detail. We present a methodology to couple atomistic and coarse-grained protein models, while solvating the atomistic part of the protein in atomistic water. This allows a free choice of which protein and solvent degrees of freedom to include atomistically, without loss of accuracy in the atomistic description. This multi-resolution methodology can successfully model stable ligand binding, and we further confirm its validity via an exploration of system properties relevant to enzymatic function. In addition to a computational speedup, such an approach can allow the identification of the essential degrees of freedom playing a role in a given process, potentially yielding new insights into biomolecular function.
The early steps of photosynthesis involve the photo-excitation of reaction centres (RCs) and light-harvesting (LH) units. Here, we show that the --historically overlooked-- excitonic delocalisation across RC and LH pigments results in a redistributio
n of dipole strengths that benefits the absorption cross section of the optical bands associated with the RC of several species. While we prove that this redistribution is robust to the microscopic details of the dephasing between these units in the purple bacterium Rhodospirillum rubrum, we are able to show that the redistribution witnesses a more fragile, but persistent, coherent population dynamics which directs excitations from the LH towards the RC units under incoherent illumination and physiological conditions. Stochastic optimisation allows us to delineate clear guidelines and develop simple analytic expressions, in order to achieve directed coherent population dynamics in artificial nano-structures.
Using methods of condensed matter and statistical physics, we examine the transport of excitons through the Fenna-Matthews-Olson (FMO) complex from a receiving antenna to a reaction center. Writing the equations of motion for the exciton creation/ann
ihilation operators, we are able to describe the exciton dynamics, even in the regime when the reorganization energy is of the order of the intra-system couplings. In particular, we obtain the well-known quantum oscillations of the site populations. We determine the exciton transfer efficiency in the presence of a quenching field and protein environment. While the majority of the protein vibronic modes are treated as a heat bath, we address the situation when specific modes are strongly coupled to excitons and examine the effects of these modes on the quantum oscillations and the energy transfer efficiency. We find that, for the vibronic frequencies below 16 meV, the exciton transfer is drastically suppressed. We attribute this effect to the formation of polaronic states where the exciton is transferred back and forth between the two pigments with the absorption/emission of the vibronic quanta, instead of proceeding to the reaction center. The same effect suppresses the quantum beating at the vibronic frequency of 25 meV. We also show that the efficiency of the energy transfer can be enhanced when the vibronic mode strongly couples to the third pigment only, instead of coupling to the entire system.
سجل دخول لتتمكن من نشر تعليقات
التعليقات
جاري جلب التعليقات
سجل دخول لتتمكن من متابعة معايير البحث التي قمت باختيارها
