Kinetics of Electron Transfer between Redox Cofactors in Photosystem I Measured by High-Frequency EPR Spectroscopy.

The kinetics of the primary electron donor P and the quinone acceptor A redox transitions were simultaneously studied for the first time in the time range of 200 μs-10 ms using high-frequency pulse Q-band EPR spectroscopy at cryogenic temperatures in various complexes of photosystem I (PSI) from the cyanobacterium PCC 6803. In the A-core PSI complexes that lack 4Fe4S clusters, the kinetics of the A and P signals disappearance at 100 K were similar and had a characteristic time of τ ≈ 500 μs, caused by charge recombination in the PA ion-radical pair in the branch of redox cofactors. The kinetics of the backward electron transfer from A to P in the branch of redox cofactors with τ < 100 μs could not be resolved due to time limitations of the method.

Exciton interactions of chlorophyll tetramer in water-soluble chlorophyll-binding protein BoWSCP.

The exciton interaction of four chlorophyll a (Chl a) molecules in a symmetrical tetrameric complex of the water-soluble chlorophyll-binding protein BoWSCP was analyzed in the pH range of 3-11. Exciton splitting ΔE = 232 ± 2 cm of the Q band of Chl a into two subcomponents with relative intensities of 78.1 ± 0.

Changes in the Electron Transfer Symmetry in the Photosystem I Reaction Centers upon Removal of Iron-Sulfur Clusters.

In photosynthetic reaction centers of intact photosystem I (PSI) complexes from cyanobacteria, electron transfer at room temperature occurs along two symmetrical branches of redox cofactors A and B at a ratio of ~3 : 1 in favor of branch A. Previously, this has been indirectly demonstrated using pulsed absorption spectroscopy and more directly by measuring the decay modulation frequencies of electron spin echo signals (electron spin echo envelope modulation, ESEEM), which allows to determine the distance between the separated charges of the primary electron donor P and phylloquinone acceptors A and A in the symmetric redox cofactors branches A and B. In the present work, these distances were determined using ESEEM in PSI complexes lacking three 4Fe-4S clusters, F, F, and F, and the PsaC protein subunit (the so-called P-A core), in which phylloquinone molecules A and A serve as the terminal electron acceptors.

Measurements of the light-induced steady state electric potential generation by photosynthetic pigment-protein complexes.

In this minireview, we consider the methods of measurements of the light-induced steady state transmembrane electric potential (Δψ) generation by photosynthetic systems, e.g. photosystem I (PS I).

The Interaction of Water-Soluble Nitroxide Radicals with Photosystem II.

In this work, we investigated the redox transients of a number of water-soluble spin labels upon their interactions with Photosystem II (PS II) core complexes isolated from spinach leaves. We have found that the reactivity of nitroxide radicals, determined by the rate of their reduction upon illumination of PS II, depends on the chemical structure of radicals and the capability of their coming close to low-potential redox centers of photoactive PS II complexes. An enhanced capability of nitroxide radicals to accept electrons from PS II correlates with their chemical structure.

Conserved residue PsaB-Trp673 is essential for high-efficiency electron transfer between the phylloquinones and the iron-sulfur clusters in Photosystem I.

Despite the high level of symmetry between the PsaA and PsaB polypeptides in Photosystem I, some amino acids pairs are strikingly different, such as PsaA-Gly693 and PsaB-Trp673, which are located near a cluster of 11 water molecules between the A and A quinones and the F iron-sulfur cluster. In this work, we changed PsaB-Trp673 to PsaB-Phe673 in Synechocystis sp. PCC 6803.

Trehalose matrix effects on electron transfer in Mn-depleted protein-pigment complexes of Photosystem II.

The kinetics of flash-induced re-reduction of the Photosystem II (PS II) primary electron donor P was studied in solution and in trehalose glassy matrices at different relative humidity. In solution, and in the re-dissolved glass, kinetics were dominated by two fast components with lifetimes in the range of 2-7 μs, which accounted for >85% of the decay. These components were ascribed to the direct electron transfer from the redox-active tyrosine Y to P.

Multiple pathways of charge recombination revealed by the temperature dependence of electron transfer kinetics in cyanobacterial photosystem I.

The kinetics of charge recombination in Photosystem I P-F/F complexes and P-F cores lacking the terminal iron‑sulfur clusters were studied over a temperatures range of 310 K to 4.2 K. Analysis of the charge recombination kinetics in this temperature range allowed the assignment of backward electron transfer from the different electron acceptors to P.

Critical evaluation of electron transfer kinetics in P-F/F, P-F, and P-A Photosystem I core complexes in liquid and in trehalose glass.

This work aims to fully elucidate the effects of a trehalose glassy matrix on electron transfer reactions in cyanobacterial Photosystem I (PS I). Forward and backward electron transfer rates from A and A to F and charge recombination rates from A, A, A, F, and [F/F] to P were measured in P-F/F complexes, P-F cores, and P-A cores, both in liquid and in a trehalose glassy matrix at 11% humidity. By comparing CONTIN-resolved kinetic events over 6 orders of time in increasingly simplified versions of PS I at 480 nm, a wavelength that reports primarily A/A oxidation, and over 9 orders of time at 830 nm, a wavelength that reports P reduction and A oxidation, assignments could be made for nearly all of the resolved kinetic phases.

Electron Transfer through the Acceptor Side of Photosystem I: Interaction with Exogenous Acceptors and Molecular Oxygen.

This review considers the state-of-the-art on mechanisms and alternative pathways of electron transfer in photosynthetic electron transport chains of chloroplasts and cyanobacteria. The mechanisms of electron transport control between photosystems (PS) I and II and the Calvin-Benson cycle are considered. The redistribution of electron fluxes between the noncyclic, cyclic, and pseudocyclic pathways plays an important role in the regulation of photosynthesis.

Interaction of various types of photosystem I complexes with exogenous electron acceptors.

Interaction of photosystem I (PS I) complexes from cyanobacteria Synechocystis sp. PCC 6803 containing various quinones in the A-site (phylloquinone PhQ in the wild-type strain (WT), and plastoquinone PQ or 2,3-dichloronaphthoquinone Cl NQ in the menB deletion strain) and different numbers of FeS clusters (intact WT and F-core complexes depleted of F/F centers) with external acceptors has been studied. The efficiency of interaction was estimated by measuring the light-induced absorption changes at 820 nm due to the reduction of the special pair of chlorophylls (P) by an external acceptor(s).

Kinetic modeling of electron transfer reactions in photosystem I complexes of various structures with substituted quinone acceptors.

The reduction kinetics of the photo-oxidized primary electron donor P in photosystem I (PS I) complexes from cyanobacteria Synechocystis sp. PCC 6803 were analyzed within the kinetic model, which considers electron transfer (ET) reactions between P, secondary quinone acceptor A, iron-sulfur clusters and external electron donor and acceptors - methylviologen (MV), 2,3-dichloro-naphthoquinone (ClNQ) and oxygen. PS I complexes containing various quinones in the A-binding site (phylloquinone PhQ, plastoquinone-9 PQ and ClNQ) as well as F -core complexes, depleted of terminal iron-sulfur F /F clusters, were studied.

Elastic Vibrations in the Photosynthetic Bacterial Reaction Center Coupled to the Primary Charge Separation: Implications from Molecular Dynamics Simulations and Stochastic Langevin Approach.

Primary electron transfer reactions in the bacterial reaction center are difficult for theoretical explication: the reaction kinetics, almost unalterable over a wide range of temperature and free energy changes, revealed oscillatory features observed initially by Shuvalov and coauthors (1997, 2002). Here the reaction mechanism was studied by molecular dynamics and analyzed within a phenomenological Langevin approach. The spectral function of polarization around the bacteriochlorophyll special pair PLPM and the dielectric response upon the formation of PL(+)PM(-) dipole within the special pair were calculated.

Age-associated murine cardiac lesions are attenuated by the mitochondria-targeted antioxidant SkQ1.

Age-related changes in mammalian hearts often result in cardiac hypertrophy and fibrosis that are preceded by inflammatory infiltration. In this paper, we show that lifelong treatment of BALB/c and C57BL/6 mice with the mitochondria-targeted antioxidant SkQ1 retards senescence-associated myocardial disease (cardiomyopathy), cardiac hypertrophy, and diffuse myocardial fibrosis. To investigate the molecular basis of the action of SkQ1, we have applied DNA microarray analysis.

Mechanism of primary and secondary ion-radical pair formation in photosystem I complexes.

The mechanisms of the ultrafast charge separation in reaction centers of photosystem I (PS I) complexes are discussed. A kinetic model of the primary reactions in PS I complexes is presented. The model takes into account previously calculated values of redox potentials of cofactors, reorganization energies of the primary P700(+)A0(-) and secondary P700(+)A1(-) ion-radical pairs formation, and the possibility of electron transfer via both symmetric branches A and B of redox-cofactors.

Molecular dynamics study of the primary charge separation reactions in Photosystem I: effect of the replacement of the axial ligands to the electron acceptor A₀.

Molecular dynamics (MD) calculations, a semi-continuum (SC) approach, and quantum chemistry (QC) calculations were employed together to investigate the molecular mechanics of ultrafast charge separation reactions in Photosystem I (PS I) of Thermosynechococcus elongatus. A molecular model of PS I was developed with the aim to relate the atomic structure with electron transfer events in the two branches of cofactors. A structural flexibility map of PS I was constructed based on MD simulations, which demonstrated its rigid hydrophobic core and more flexible peripheral regions.