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Molecular hydrogen, H2, is an energy carrier that is increasing in popularity as an alternative fuel. Presently, the major part of commercially available H2 is produced from fossil resources. To make H2 a true contender to fossil fuels, a sustainable production via water splitting by renewable electricity in combination with earth-abundant catalysts or by photosynthetic microorganisms is required.

Organic carbonyl compounds have been considered as promising alternatives to traditional inorganic battery materials due to their low-cost, sustainability and structural diversity. The development of carbonyl compounds as energy storage materials is, however, hampered by dissolution as well as by the low electronic conductivity of these materials. Herein a conducting redox polymer concept is employed where the carbonyl group is functionalized onto a conducting polymer. The utilization of a conducting polymer prevents the dissolution and provides electron transport pathways to support the carbonyl group redox reaction. A high potential quinizarin (Qz) is used as capacity-carrying group. It is functionalized onto a thiophene-based trimer unit which is polymerized through a post-deposition polymerization method. In the resulting material, Qz is redox-matched with the conducting polymer backbone and exhibits two reversible 1e/1Li+ redox processes at 3.1 and 3.4 V vs. Li+/0, respectively. Together with a lithium metal anode, a battery cell with an average discharge voltage of 3.3 V, a discharge capacity of 65 mAh/g at 1.5 C and a capacity retention of 74% after 500 cycles is assembled.

The coordination of a substrate water molecule on a metal centered catalyst for water oxidation is a crucial step involving the reorganization of the ligand sphere. This process can occur by substi ...

The tyrosine residue D2-Tyr160 (Tyr(D)) in photosystem II (PSII) can be oxidized through charge equilibrium with the oxygen evolving complex in PSII. The kinetics of the electron transfer from Tyr( ...

Photosystem II is a protein complex embedded in the thylakoid membrane of photosynthetic organisms and performs the light driven water oxidation into electrons and molecular oxygen that initiate the photosynthetic process. This important complex is composed of more than two dozen of intrinsic and peripheral subunits, of those half are low molecular mass proteins. PsbY is one of those low molecular mass proteins; this 4.7-4.9kDa intrinsic protein seems not to bind any cofactors. Based on structural data from cyanobacterial and red algal Photosystem II PsbY is located closely or in direct contact with cytochrome b559. Cytb559 consists of two protein subunits (PsbE and PsbF) ligating a heme-group in-between them. While the exact function of this component in Photosystem II has not yet been clarified, a crucial role for assembly and photo-protection in prokaryotic complexes has been suggested. One unique feature of Cytb559 is its redox-heterogeneity, forming high, medium and low potential, however, neither origin nor mechanism are known. To reveal the function of PsbY within Photosystem II of Arabidopsis we have analysed PsbY knock-out plants and compared them to wild type and to complemented mutant lines. We show that in the absence of PsbY protein Cytb559 is only present in its oxidized, low potential form and plants depleted of PsbY were found to be more susceptible to photoinhibition.

Redox properties of the acceptor side of Photosystem II were studied during H 2 gas production in cells of Chlamydomonas reinhardtii. Flash-induced variable fluorescence changes and thermoluminescence measurements were performed in wild type and Stm6 mutant cells during different stages of sulfur (S)-deprivation. Analysis of the fluorescence decay kinetics indicated that the forward electron transfer on the acceptor side of Photosystem II was dramatically slowed down during the O 2 evolution and O 2 consumption stages and was completely blocked in the anaerobic stage of S-deprivation, thus, indicating a complete reduction of the PQ-pool. During the H 2 formation stage, the forward electron transfer kinetics in the μsec and msec time scale re-appeared indicating partially restored electron flow from Q A − to Q B and the PQ-pool. Thermoluminescese measurements fully confirmed the fluorescence kinetic analysis. Activation of hydrogenase in the H 2 formation stage is responsible for re-oxidation of the PQ pool and reactivation of the electron flow which was found to be faster and more efficient on the Stm6 mutant due to the higher amount of functionally preserved Photosystem II.

Titanium dioxide samples were prepared in the presence of different amounts of fluorine via hydrothermal method. It has been found that the presence of fluoride influenced the physico-chemical properties of TiO2 in various ways as polymorphic form stability, surface hydroxylation, generation of hydroxyl radicals under irradiation and formation of Ti3+ centers and oxygen vacancies. The generation rate of OH radicals was investigated by the photoluminescence technique in the presence of terephthalic acid. X-ray diffractometry indicated that fluorine stabilized the anatase TiO2. X-Ray photoelectron spectroscopy (XPS) revealed the presence of fluorine on the surface and the shift of the valence band edge towards less negative potentials, electron paramagnetic resonance (EPR) confirmed the formation of Ti3+ in the bulk of the photocatalysts, UV–vis spectra showed the extension of the TiO2 photo-response in the visible light region. 2-Propanol degradation and 4-methoxybenzyl alcohol partial oxidation were studied as probe reactions by using the home prepared powders as photocatalysts. Surprisingly, the photocatalytic activity resulted to be mainly affected by OH radicals formation ability under irradiation, rather than by the presence of {0 0 1} facets, although it cannot be excluded that the latter could influence the ability to form radicals under irradiation.

The far-red limit of photosystem I (PS I) photochemistry was studied by EPR spectroscopy using laser flashes between 730 and 850 nm. In manganese-depleted spinach thylakoid membranes, the primary donor in PS I, P700, was oxidized simultaneously with tyrosine Z, the secondary donor in PS II. It was found that at 295 K PS I photochemistry, observed as P700+ formation, was functional up to 840 nm. This is 30 nm further to the red region than was reported for PS II photochemistry (Thapper, A., Mamedov, F., Mokvist, F., Hammarstrom, L., and Styring, S. (2009) Plant Cell 21, 2391–2401). The same far-red limit for the P700+ formation was observed in a PS I reaction center core preparation from Nostoc punctiforme. The reduction of the acceptor side of PS I, observed as reduction of the iron-sulfur centers FA and FB by low temperature EPR measurements, was also functional at 15 K with light up to >830 nm. Taken together, these results, obtained from both plants and cyanobacteria, most likely rule out involvement of the red-absorbing antenna chlorophylls in this reaction. Instead we propose the existence of weak charge transfer bands absorbing in the far-red region in the ensemble of excitonically coupled chlorophyll a molecules around P700 similar to what has been found in the reaction center of PS II. These charge transfer bands could be responsible for the far-red light absorption leading to PS I photochemistry at wavelengths up to 840 nm.

Metalloradical EPR signals have been found in intact Photosystem II at cryogenic temperatures. They reflect the light-driven formation of the tyrosine Z radical (Y(Z)) in magnetic interaction with the CaMn(4) cluster in a particular S state. These so-called split EPR signals, induced at cryogenic temperatures, provide means to study the otherwise transient Y(Z) and to probe the S states with EPR spectroscopy. In the S(0) and S(1) states, the respective split signals are induced by illumination of the sample in the visible light range only. In the S(3) state the split EPR signal is induced irrespective of illumination wavelength within the entire 415-900nm range (visible and near-IR region) [Su, J. H., Havelius, K. G. V., Ho, F. M., Han, G., Mamedov, F., and Styring, S. (2007) Biochemistry 46, 10703-10712]. An important question is whether a single mechanism can explain the induction of the Split S(3) signal across the entire wavelength range or whether wavelength-dependent mechanisms are required. In this paper we confirm that the Y(Z) radical formation in the S(1) state, reflected in the Split S(1) signal, is driven by P680-centered charge separation. The situation in the S(3) state is different. In Photosystem II centers with pre-reduced quinone A (Q(A)), where the P680-centered charge separation is blocked, the Split S(3) EPR signal could still be induced in the majority of the Photosystem II centers using both visible and NIR (830nm) light. This shows that P680-centered charge separation is not involved. The amount of oxidized electron donors and reduced electron acceptors (Q(A)(-)) was well correlated after visible light illumination at cryogenic temperatures in the S(1) state. This was not the case in the S(3) state, where the Split S(3) EPR signal was formed in the majority of the centers in a pathway other than P680-centered charge separation. Instead, we propose that one mechanism exists over the entire wavelength interval to drive the formation of the Split S(3) signal. The origin for this, probably involving excitation of one of the Mn ions in the CaMn(4) cluster in Photosystem II, is discussed.

Phosphorylation-dependent movement of the light-harvesting complex II (LHCII) between photosystem II (PSII) and photosystem I (PSI) takes place in order to balance the function of the two photosystems. Traditionally, the phosphorylatable fraction of LHCII has been considered as the functional unit of this dynamic regulation. Here, a mechanical fractionation of the thylakoid membrane of Spinacia oleracea was performed from leaves both in the phosphorylated state (low light, LL) and in the dephosphorylated state (dark, D) in order to compare the phosphorylation-dependent protein movements with the excitation changes occurring in the two photosystems upon LHCII phosphorylation. Despite the fact that several LHCII proteins migrate to stroma lamellae when LHCII is phosphorylated, no increase occurs in the 77 K fluorescence emitted from PSI in this membrane fraction. On the contrary, such an increase in fluorescence occurs in the grana margin fraction, and the functionally important mobile unit is the PSI–LHCI complex. A new model for LHCII phosphorylation driven regulation of relative PSII/PSI excitation thus emphasises an increase in PSI absorption cross-section occurring in grana margins upon LHCII phosphorylation and resulting from the movement of PSI–LHCI complexes from stroma lamellae and subsequent co-operation with the P-LHCII antenna from the grana. The grana margins probably give a flexibility for regulation of linear and cyclic electron flow in plant chloroplasts.

The functional state of the Photosystem (PS) II complex in Arabidopsis psbR T-DNA insertion mutant was studied. The DeltaPsbR thylakoids showed about 34% less oxygen evolution than WT, which correlates with the amounts of PSII estimated from Y(D)(ox) radical EPR signal. The increased time constant of the slow phase of flash fluorescence (FF)-relaxation and upshift in the peak position of the main TL-bands, both in the presence and in the absence of DCMU, confirmed that the S(2)Q(A)(-) and S(2)Q(B)(-) charge recombinations were stabilized in DeltaPsbR thylakoids. Furthermore, the higher amount of dark oxidized Cyt-b559 and the increased proportion of fluorescence, which did not decay during the 100s time span of the measurement thus indicating higher amount of Y(D)(+)Q(A)(-) recombination, pointed to the donor side modifications in DeltaPsbR. EPR measurements revealed that S(1)-to-S(2)-transition and S(2)-state multiline signal were not affected by mutation. The fast phase of the FF-relaxation in the absence of DCMU was significantly slowed down with concomitant decrease in the relative amplitude of this phase, indicating a modification in Q(A) to Q(B) electron transfer in DeltaPsbR thylakoids. It is concluded that the lack of the PsbR protein modifies both the donor and the acceptor side of the PSII complex.

The long-lived, light-induced radical Y-D(.) of the Tyr161 residue in the D2 protein of Photosystem 11 (PSII) is known to magnetically interact with the CaMn4 cluster, situated similar to 30 angstrom away. In this study we report a transient step-change increase in YD EPR intensity upon the application of a single laser flash to S, state-synchronised PSII-enriched membranes from spinach. This transient effect was observed at room temperature and high applied microwave power (100 mW) in samples containing PpBQ, as well as those containing DCMU. The subsequent decay lifetimes were found to differ depending on the additive used. We propose that this flash-induced signal increase was caused by enhanced spin relaxation of YD by the OEC in the S-2 state, as a consequence of the single laser flash turnover. The post-flash decay reflected S-2 -> S-1 back-turnover, as confirmed by their correlations with independent measurements of S-2 multiline EPR signal and flash-induced variable fluorescence decay kinetics under corresponding experimental conditions. This flash-induced effect opens up the possibility to study the kinetic behaviour of S-state transitions at room temperature using YD as a probe. (c) 2006 Elsevier B.Z. All rights reserved. (Less)

The supramolecular organization of photosystem II (PSII) was characterized in distinct domains of the thylakoid membrane, the grana core, the grana margins, the stroma lamellae, and the so-called Y100 fraction. PSII supercomplexes, PSII core dimers, PSII core monomers, PSII core monomers lacking the CP43 subunit, and PSII reaction centers were resolved and quantified by blue native PAGE, SDS-PAGE for the second dimension, and immunoanalysis of the D1 protein. Dimeric PSII (PSII supercomplexes and PSII core dimers) dominate in the core part of the thylakoid granum, whereas the monomeric PSII prevails in the stroma lamellae. Considerable amounts of PSII monomers lacking the CP43 protein and PSII reaction centers (D1-D2-cytochrome b559 complex) were found in the stroma lamellae. Our quantitative picture of the supramolecular composition of PSII, which is totally different between different domains of the thylakoid membrane, is discussed with respect to the function of PSII in each fraction. Steady state electron transfer, flash-induced fluorescence decay, and EPR analysis revealed that nearly all of the dimeric forms represent oxygen-evolving PSII centers. PSII core monomers were heterogeneous, and a large fraction did not evolve oxygen. PSII monomers without the CP43 protein and PSII reaction centers showed no oxygen-evolving activity.

The oxygen-evolving complex of eukaryotic photosystem II (PSII) consists of three extrinsic nuclear-encoded subunits, PsbO (33 kDa), PsbP (23 kDa), and PsbQ (17 kDa). Additionally, the 10-kDa PsbR protein has been found in plant PSII and anticipated to play a role in water oxidation, yet the physiological significance of PsbR has remained obscure. Using the Arabidopsis psbR mutant, we showed that the light-saturated rate of oxygen evolution is strongly reduced in the absence of PsbR, particularly in low light-grown plants. Lack of PsbR also induced a reduction in the content of both the PsbP and the PsbQ proteins, and a near depletion of these proteins was observed under steady state low light conditions. This regulation occurred post-transcriptionally and likely involves a proteolytic degradation of the PsbP and PsbQ proteins in the absence of an assembly partner, proposed to be the PsbR protein. Stable assembly of PsbR in the PSII core complex was, in turn, shown to require a chloroplast-encoded intrinsic low molecular mass PSII subunit PsbJ. Our results provided evidence that PsbR is an important link in the PSII core complex for stable assembly of the oxygen-evolving complex protein PsbP, whereas the effects on the assembly of PsbQ are probably indirect. The physiological role of the PsbR, PsbP, and PsbQ proteins is discussed in light of their peculiar expression in response to growth light conditions.

Many heavy metals inhibit electron transfer reactions in Photosystem II (PSII). Cd2+ is known to exchange, with high affinity in a slow reaction, for the Ca2+ cofactor in the Ca/Mn cluster that constitutes the oxygen-evolving center. This results in inhibition of photosynthetic oxygen evolution. There are also indications that Cd2+ binds to other sites in PSII, potentially to proton channels in analogy to heavy metal binding in photosynthetic reaction centers from purple bacteria. In search for the effects of Cd2+-binding to those sites, we have studied how Cd2+ affects electron transfer reactions in PSII after short incubation times and in sites, which interact with Cd2+ with low affinity. Overall electron transfer and partial electron transfer were studied by a combination of EPR spectroscopy of individual redox components, flash-induced variable fluorescence and steady state oxygen evolution measurements. Several effects of Cd2+ were observed: (i) the amplitude of the flash-induced variable fluorescence was lost indicating that electron transfer from Y-Z to P-680(+) was inhibited; (ii) Q(A)(-) to Q(B) electron transfer was slowed down; (iii) the S-2 state multiline EPR signal was not observable; (iv) steady state oxygen evolution was inhibited in both a high-affinity and a low-affinity site; (v) the spectral shape of the EPR signal from Q(A)(-)Fe(2+) was modified but its amplitude was not sensitive to the presence of Cd2+. In addition, the presence of both Ca2+ and DCMU abolished Cd2+-induced effects partially and in different sites. The number of sites for Cd2+ binding and the possible nature of these sites are discussed. (C) 2004 Elsevier B.V. All rights reserved. (Less)

The spin-state of cytochrome b559 (Cyt b559) was studied in photosystem II (PSII) membrane fragments by low-temperature EPR spectroscopy. Treatment of the membranes with 2,3-dichloro-5,6-dicyano-p-benzoquinone (DDQ) converts the native low-spin (LS) form of Cyt b559 to the high-spin (HS) form characterized with the g= 6.19 and g= 5.95 split signal. The HS Cyt b559 was pH dependent with the amplitude increasing toward more acidic pH values (pH 5.5-8.5). The HS state was not photochemically active upon 77 and 200 K continuous illumination under our conditions and was characterized by a low reduction potential (=

In vivo photoactivation of Photosystem II was studied in the FUD39 mutant strain of the green alga Chlamydomonas reinhardtii which lacks the 23 kDa protein subunit involved in water oxidation. Dark grown cells, devoid of oxygen evolution, were illuminated at 0.8 μE m−2 s−1 light intensity which promotes optimal activation of oxygen evolution, or at 17 μE m−2 s−1, where photoactivation compete with deleterious photodamage. The involvement of the two redox active cofactors tyrosineD and cytochrome b559 during the photoactivation process, was investigated by EPR spectroscopy. TyrosineD on the D2 reaction center protein functions as auxiliary electron donor to the primary donor P680+ during the first minutes of photoactivation at 0.8 μE m−2 s−1 (compare with Rova et al., Biochemistry, 37 (1998) 11039–11045.). Here we show that also cytochrome b559 was rapidly oxidized during the first 10 min of photoactivation with a similar rate to tyrosineD. This implies that both cytochrome b559 and tyrosineD may function as auxiliary electron donors to P680+ and/or the oxidized tyrosine⋅Z on the D1 protein, to avoid photoinhibition before successful photoactivation was accomplished. As the catalytic water-oxidation successively became activated, TyrosineD remained oxidized while cytochrome b559 became rereduced to the equilibrium level that was observed prior to photoactivation. At 17 μE m−2 s−1 light intensity, where photoinhibition competes significantly with photoactivation, tyrosineD was very rapidly completely oxidized, after which the amount of oxidized tyrosineD decreased due to photoinhibition. In contrast, cytochrome b559 became reduced during the first 2 min of photoactivation at 17 μE m−2 s−1. After this, it was reoxidized, returning to the equilibrium level within 10 min. Thus, during in vivo photoactivation in high-light cytochrome b559 serves two functions. Initially, it probably oxidizes the reduced primary acceptor pheophytin, thereby relieving the acceptor side of reductive pressure, and later on it serves as auxiliary electron donor, preventing donor-side photoinhibition.