Photochemistry in the isolated Photosystem II reaction-centre core complex.
Ontology highlight
ABSTRACT:
SUBMITTER: Demetriou C
PROVIDER: S-EPMC1149238 | biostudies-other | 1988 Jun
REPOSITORIES: biostudies-other
Similar Datasets
Project description:The photosystem II reaction centre is the photosynthetic complex responsible for oxygen production on Earth. Its water splitting function is particularly favoured by the formation of a stable charge separated state via a pathway that starts at an accessory chlorophyll. Here we envision a photovoltaic device that places one of these complexes between electrodes and investigate how the mean current and its fluctuations depend on the microscopic interactions underlying charge separation in the pathway considered. Our results indicate that coupling to well resolved vibrational modes does not necessarily offer an advantage in terms of power output but can lead to photo-currents with suppressed noise levels characterizing a multi-step ordered transport process. Besides giving insight into the suitability of these complexes for molecular-scale photovoltaics, our work suggests a new possible biological function for the vibrational environment of photosynthetic reaction centres, namely, to reduce the intrinsic current noise for regulatory processes.
| S-EPMC5636947 | biostudies-literature
Project description:LC-MS/MS identification of small subunit peptides of Photosystem II assembly intermediate (NRC) with/without trypsin digestion. Peptide sequence identification with HCD fragmentation using Q-Exactive plus mass spectrometer (Thermo-Fisher)
2019-10-14 | PXD013406 | Pride
Project description:Photosystem II (PSII) is a membrane-spanning, multi-subunit pigment-protein complex responsible for the oxidation of water and the reduction of plastoquinone in oxygenic photosynthesis. In the present review, the recent explosive increase in available structural information about the PSII core complex based on X-ray crystallography and cryo-electron microscopy is described at a level of detail that is suitable for a future structure-based analysis of light-harvesting processes. This description includes a proposal for a consistent numbering scheme of protein-bound pigment cofactors across species. The structural survey is complemented by an overview of the state of affairs in structure-based modeling of excitation energy transfer in the PSII core complex with emphasis on electrostatic computations, optical properties of the reaction center, the assignment of long-wavelength chlorophylls, and energy trapping mechanisms.
| S-EPMC7184784 | biostudies-literature
Project description:The fluorescence kinetics of cyanobacterial photosystem II (PSII) core particles with closed reaction centers (RCs) were studied with picosecond resolution. The data are modeled in terms of electron transfer (ET) and associated protein conformational relaxation processes, resolving four different radical pair (RP) states. The target analyses reveal the importance of protein relaxation steps in the ET chain for the functioning of PSII. We also tested previously published data on cyanobacterial PSII with open RCs using models that involved protein relaxation steps as suggested by our data on closed RCs. The rationale for this reanalysis is that at least one short-lived component could not be described in the previous simpler models. This new analysis supports the involvement of a protein relaxation step for open RCs as well. In this model the rate of ET from reduced pheophytin to the primary quinone Q(A) is determined to be 4.1 ns(-1). The rate of initial charge separation is slowed down substantially from approximately 170 ns(-1) in PSII with open RCs to 56 ns(-1) upon reduction of Q(A). However, the free-energy drop of the first RP is not changed substantially between the two RC redox states. The currently assumed mechanistic model, assuming the same early RP intermediates in both states of RC, is inconsistent with the presented energetics of the RPs. Additionally, a comparison between PSII with closed RCs in isolated cores and in intact cells reveals slightly different relaxation kinetics, with a approximately 3.7 ns component present only in isolated cores.
| S-EPMC2716457 | biostudies-literature
Project description:Calcium enhances turfgrass response to salt stress. However, little is known about PSII photochemical changes when exogenous calcium was applied in salinity-stressed turfgrass. Here, we probe into the rearrangements of PSII electron transport and endogenous ion accumulation in tall fescue (Festuca arundinacea Schreber) treated with exogenous calcium under salt stress. Three-month-old seedlings of genotype "TF133" were subjected to the control (CK), salinity (S), salinity + calcium nitrate (SC), and salinity + ethylene glycol tetraacetic acid (SE). Calcium nitrate and ethylene glycol tetraacetic acid was used as exogenous calcium donor and calcium chelating agent respectively. At the end of a 5-day duration treatment, samples in SC regime had better photochemistry performance on several parameters than salinity only. Such as the Area (equal to the plastoquinone pool size), N (number of [Formula: see text] redox turnovers until Fm is reached), ?E0, or ?Ro (Efficiencdy/probability with which a PSII trapped electron is transferred from QA to QB or PSI acceptors), ABS/RC (Absorbed photon flux per RC). All the above suggested that calcium enhanced the electron transfer of PSII (especially beyond [Formula: see text]) and prevented reaction centers from inactivation in salt-stressed tall fescue. Furthermore, both grass shoot and root tissues generally accumulated more C, N, Ca2+, and K+ in the SC regime than S regime. Interrelated analysis indicated that ?E0, ?Ro, ABS/RC, C, and N content in shoots was highly correlated to each other and significantly positively related to Ca2+ and K+ content in roots. Besides, high salt increased ATP6E and CAMK2 transcription level in shoot at 1 and 5 day, respectively while exogenous calcium relieved it. In root, CAMK2 level was reduced by Salinity at 5 day and exogenous calcium recovered it. These observations involved in electron transport capacity and ion accumulation assist in understanding better the protective role of exogenous calcium in tall fescue under salt stress.
| S-EPMC5715236 | biostudies-literature
Project description:Five-day exposure of clary sage (Salvia sclarea L.) to 100 μM cadmium (Cd) in hydroponics was sufficient to increase Cd concentrations significantly in roots and aboveground parts and affect negatively whole plant levels of calcium (Ca) and magnesium (Mg), since Cd competes for Ca channels, while reduced Mg concentrations are associated with increased Cd tolerance. Total zinc (Zn), copper (Cu), and iron (Fe) uptake increased but their translocation to the aboveground parts decreased. Despite the substantial levels of Cd in leaves, without any observed defects on chloroplast ultrastructure, an enhanced photosystem II (PSII) efficiency was observed, with a higher fraction of absorbed light energy to be directed to photochemistry (ΦPSΙΙ). The concomitant increase in the photoprotective mechanism of non-photochemical quenching of photosynthesis (NPQ) resulted in an important decrease in the dissipated non-regulated energy (ΦNO), modifying the homeostasis of reactive oxygen species (ROS), through a decreased singlet oxygen (1O2) formation. A basal ROS level was detected in control plant leaves for optimal growth, while a low increased level of ROS under 5 days Cd exposure seemed to be beneficial for triggering defense responses, and a high level of ROS out of the boundaries (8 days Cd exposure), was harmful to plants. Thus, when clary sage was exposed to Cd for a short period, tolerance mechanisms were triggered. However, exposure to a combination of Cd and high light or to Cd alone (8 days) resulted in an inhibition of PSII functionality, indicating Cd toxicity. Thus, the rapid activation of PSII functionality at short time exposure and the inhibition at longer duration suggests a hormetic response and describes these effects in terms of "adaptive response" and "toxicity", respectively.
| S-EPMC7793146 | biostudies-literature
Project description:Cyanobacteria living in the harsh environment of the desert have to protect themselves against high light intensity and prevent photodamage. These cyanobacteria are in a desiccated state during the largest part of the day when both temperature and light intensity are high. In the desiccated state, their photosynthetic activity is stopped, whereas upon rehydration the ability to perform photosynthesis is regained. Earlier reports indicate that light-induced excitations in Leptolyngbya ohadii are heavily quenched in the desiccated state, because of a loss of structural order of the light-harvesting phycobilisome structures (Bar Eyal et al. in Proc Natl Acad Sci 114:9481, 2017) and via the stably oxidized primary electron donor in photosystem I, namely P700+ (Bar Eyal et al. in Biochim Biophys Acta Bioenergy 1847:1267-1273, 2015). In this study, we use picosecond fluorescence experiments to demonstrate that a third protection mechanism exists, in which the core of photosystem II is quenched independently.
| S-EPMC6930311 | biostudies-literature
Project description:Oxygenic photosynthesis begins in the reaction center (RC) of the protein complex photosystem II (PSII). PSII has an intriguing, nearly symmetrical arrangement of cofactors within its RC. Despite this symmetry, evolution has favored only one of the two branches of PSII for efficient electron transfer. Current spectroscopic experiments explore the electronic dynamics during the picoseconds after energy has entered the RC and until the electron transfers to the pheophytin of the first branch. We present state-of-the-art multiconfigurational multireference calculations of the excitation energies or site energies of the four chlorophyll pigments of the RC without protein environment considerations. We see a significant variation that breaks the apparent symmetry of the RC. The inner chlorophyll of the productive RC branch possessed the lowest excitation energy of the four central chlorophylls. Our computational method used here is expensive; thus, geometry optimization of the crystal structure is currently not possible. In future work, charge and energy dynamics within the RC will be included as well as a dynamic description of the protein environment and its coupling to the RC. Other state-of-the-art studies of the RC, at lower levels of electronic structure, include a static treatment of the protein environment. These almost unanimously report that the outer chlorophyll of the active branch had the lowest excitation energy. Future work is needed to reconcile this discrepancy.
| S-EPMC10851264 | biostudies-literature
Project description:Despite the apparent similarity between the plant Photosystem II reaction center (RC) and its purple bacterial counterpart, we show in this work that the mechanism of charge separation is very different for the two photosynthetic RCs. By using femtosecond visible-pump-mid-infrared probe spectroscopy in the region of the chlorophyll ester and keto modes, between 1,775 and 1,585 cm(-1), with 150-fs time resolution, we show that the reduction of pheophytin occurs on a 0.6- to 0.8-ps time scale, whereas P+, the precursor state for water oxidation, is formed after approximately 6 ps. We conclude therefore that in the Photosystem II RC the primary charge separation occurs between the "accessory chlorophyll" Chl(D1) and the pheophytin on the so-called active branch.
| S-EPMC1196200 | biostudies-literature
Project description:The laboratory synthesis of the oxygen-evolving complex (OEC) of photosystem II has been the objective of synthetic chemists since the early 1970s. However, the absence of structural information on the OEC has hampered these efforts. Crystallographic reports on photosystem II that have been appearing at ever-improving resolution over the past ten years have finally provided invaluable structural information on the OEC and show that it comprises a [Mn(3)CaO(4)] distorted cubane, to which is attached a fourth, external Mn atom, and the whole unit attached to polypeptides primarily by aspartate and glutamate carboxylate groups. Such a heterometallic Mn/Ca cubane with an additional metal attached to it has been unknown in the literature. This paper reports the laboratory synthesis of such an asymmetric cubane-containing compound with a bound external metal atom, [(1)]. All peripheral ligands are carboxylate or carboxylic acid groups. Variable-temperature magnetic susceptibility data have established 1 to possess an S = 9/2 ground state. EPR spectroscopy confirms this, and the Davies electron nuclear double resonance data reveal similar hyperfine couplings to those of other Mn(IV) species, including the OEC S(2) state. Comparison of the X-ray absorption data with those for the OEC reveal 1 to possess structural parameters that make it a close structural model of the asymmetric-cubane OEC unit. This geometric and electronic structural correspondence opens up a new front in the multidisciplinary study of the properties and function of this important biological unit.
| S-EPMC3289351 | biostudies-literature