RESUMO
Photosynthetic green sulfur bacteria are able to survive under extreme low light conditions. Nevertheless, the light-harvesting efficiencies reported so far, in particular for Fenna-Matthews-Olson (FMO) protein-reaction center complex (RCC) supercomplexes, are much lower than for photosystems of other species. Here, we approach this problem with a structure-based theory. Compelling evidence for a light-harvesting efficiency around 95% is presented for native (anaerobic) conditions that can drop down to 47% when the FMO protein is switched into a photoprotective mode in the presence of molecular oxygen. Light-harvesting bottlenecks are found between the FMO protein and the RCC, and the antenna of the RCC and its reaction center (RC) with forward energy transfer time constants of 39 ps and 23 ps, respectively. The latter time constant removes an ambiguity in the interpretation of time-resolved spectra of RCC probing primary charge transfer and provides strong evidence for a transfer-to-the trap limited kinetics of excited states. Different factors influencing the light-harvesting efficiency are investigated. A fast primary electron transfer in the RC is found to be more important for a high efficiency than the site energy funnel in the FMO protein, quantum effects of nuclear motion, or variations in the mutual orientation between the FMO protein and the RCC.
Assuntos
Carcinoma de Células Renais , Chlorobi , Neoplasias Renais , Humanos , Complexos de Proteínas Captadores de Luz/metabolismo , Proteínas de Bactérias/metabolismoRESUMO
The intermolecular contribution to the spectral density of the exciton-vibrational coupling of the homotrimeric Fenna-Matthews-Olson (FMO) light-harvesting protein of green sulfur bacteria P. aestuarii is analyzed by combining a normal mode analysis of the protein with the charge density coupling method for the calculation of local transition energies of the pigments. Correlations in site energy fluctuations across the whole FMO trimer are found at low vibrational frequencies. Including, additionally, the high-frequency intrapigment part of the spectral density, extracted from line-narrowing spectra, we study intra- and intermonomer exciton transfer. Whereas the intrapigment part of the spectral density is important for fast intramonomer exciton relaxation, the intermolecular contributions (due to pigment-environment coupling) determine the intermonomer exciton transfer. Neither the variations of the local Huang-Rhys factors nor the correlations in site energy fluctuations have a critical influence on energy transfer. At room temperature, the intermonomer transfer in the FMO protein occurs on a 10 ps time scale, whereas intramonomer exciton equilibration is roughly two orders of magnitude faster. At cryogenic temperatures, intermonomer transfer limits the lifetimes of the lowest exciton band. The lifetimes are found to increase between 20 ps in the center of this band up to 100 ps toward lower energies, which is in very good agreement with the estimates from hole burning data. Interestingly, exciton delocalization in the FMO monomers is found to slow down intermonomer energy transfer, at both physiological and cryogenic temperatures.
Assuntos
Proteínas de Bactérias/química , Complexos de Proteínas Captadores de Luz/química , Proteínas de Bactérias/metabolismo , Transferência de Energia , Complexos de Proteínas Captadores de Luz/metabolismo , Modelos Químicos , Teoria QuânticaRESUMO
We present a microscopic theory for the description of fluctuation-induced excitation energy transfer in chromophore dimers to explain experimental data on a perylene biscarboximide dyad with orthogonal transition dipole moments. Our non-Condon extension of Förster theory takes into account the fluctuations of excitonic couplings linear and quadratic in the normal coordinates, treated microscopically by quantum chemical/electrostatic calculations. The modulation of the optical transition energies of the chromophores is inferred from optical spectra of the isolated chromophores. The application of the theory to the considered dyad reveals a two to three order of magnitude increase in the rate constant by non-Condon effects. These effects are found to be dominated by fluctuations linear in the normal coordinates and provide a structure-based qualitative interpretation of the experimental time constant for energy transfer as well as its dependence on temperature.
RESUMO
Manufacturing systems are becoming increasingly complex as more advanced and emerging technologies are integrated into the factory floor to yield new processes or increase the efficiency of existing processes. As greater complexity is formed across the factory, new relationships are often generated that can lead to advanced capabilities, yet produce unforeseen faults and failures. Industrial robot arm work cells within the manufacturing environment present increasing complexity, emergent technologies, new relationships, and unpredicted faults/failures. To maintain required levels of productivity, process quality, and asset availability, manufacturers must reconcile this complexity to understand how the health degradation of constituent physical elements and functional tasks impact one another through the monitoring of critical informative measures and metrics. This article presents the initial efforts in developing a novel hierarchical decomposition methodology. The innovation in this method is that it provides the manufacturer with sufficient discretion to physically deconstruct their system and functionally decompose their process to user-defined levels based upon desired monitoring, maintenance, and control levels. This enables the manufacturer to specify relationships within and across the physical, functional, and information domains to identify impactful health degradations without having to know all possible failure modes. The hierarchical decomposition methodology will advance the state of the art in terms of improving machine health by highlighting how health degradations propagate through the relationship network prior to a piece of equipment compromising the productivity or quality of a process. The first two steps of the methodology, physical decomposition and functional decomposition, are defined in detail and applied to a multi-robot work cell use case.
RESUMO
We report a method for the structure-based calculation of the spectral density of the pigment-protein coupling in light-harvesting complexes that combines normal-mode analysis with the charge density coupling (CDC) and transition charge from electrostatic potential (TrEsp) methods for the computation of site energies and excitonic couplings, respectively. The method is applied to the Fenna-Matthews-Olson (FMO) protein in order to investigate the influence of the different parts of the spectral density as well as correlations among these contributions on the energy transfer dynamics and on the temperature-dependent decay of coherences. The fluctuations and correlations in excitonic couplings as well as the correlations between coupling and site energy fluctuations are found to be 1 order of magnitude smaller in amplitude than the site energy fluctuations. Despite considerable amplitudes of that part of the spectral density which contains correlations in site energy fluctuations, the effect of these correlations on the exciton population dynamics and dephasing of coherences is negligible. The inhomogeneous charge distribution of the protein, which causes variations in local pigment-protein coupling constants of the normal modes, is responsible for this effect. It is seen thereby that the same building principle that is used by nature to create an excitation energy funnel in the FMO protein also allows for efficient dissipation of the excitons' excess energy.