Sensitivity of the photosynthetic apparatus to UV-A radiation: role of light-harvesting complex II–photosystem II supercomplex organization

In this work we study the effect of UV-A radiation on the function of the photosynthetic apparatus in thylakoid membranes with different organization of the light-harvesting complex II–photosystem II (LHCII–PSII) supercomplex. Leaves and isolated thylakoid membranes from a number of previously characterized pea species with different LHCII size and organization were subjected to UV-A treatment. A relationship was found between the molecular organization of the LHCII (ratio of the oligomeric to monomeric forms of LHCII) and UV-A-induced changes both in the energy transfer from PSII to PSI and between the chlorophyll–protein complexes within the LHCII–PSII supercomplex. Dependence on the organization of the LHCII was also found with regard to the degree of inhibition of the photosynthetic oxygen evolution. The susceptibility of energy transfer and oxygen evolution to UV-A radiation decreased with increasing LHCII oligomerization when the UV-A treatment was performed on isolated thylakoid membranes, in contrast to the effect observed in thylakoid membranes isolated from pre-irradiated pea leaves. The data suggest that UV-A radiation leads mainly to damage of the PSIIα centers. Comparison of membranes with different organization of their LHCII–PSII supercomplex shows that the oligomeric forms of LHCII play a key role for sensitivity to UV-A radiation of the photosynthetic apparatus. S. G. Taneva is Associated member of the Institute of Biophysics, Bulgarian Academy of Sciences.     

Voltage changes involving photosystem II quinone–iron complex turnover

An electrometrical technique was used to investigate proton-coupled electron transfer between the primary plastoquinone acceptor Q_A⁻ and the oxidized non-heme iron Fe³⁺ on the acceptor side of photosystem II core particles incorporated into phospholipid vesicles. The sign of the transmembrane electric potential difference Δψ (negative charging of the proteoliposome interior) indicates that the iron–quinone complex faces the interior surface of the proteoliposome membrane. Preoxidation of the non-heme iron was achieved by addition of potassium ferricyanide entrapped into proteoliposomes. Besides the fast unresolvable kinetic phase (τ ∼ 0.1 μs) of Δψ generation related to electron transfer between the redox-active tyrosine Y_Z and Q_A, an additional phase in the submillisecond time domain (τ ∼ 0.1 ms at 23°C, pH 7.0) and relative amplitude ∼ 20% of the amplitude of the fast phase was observed under exposure to the first flash. This phase was absent under the second laser flash, as well as upon the first flash in the presence of DCMU, an inhibitor of electron transfer between Q_A and the secondary quinone Q_B. The rate of the additional electrogenic phase is decreased by about one-half in the presence of D₂O and is reduced with the temperature decrease. On the basis of the above observations we suggest that the submillisecond electrogenic reaction induced by the first flash is due to the vectorial transfer of a proton from external aqueous phase to an amino acid residue(s) in the vicinity of the non-heme iron. The possible role of the non-heme iron in cyclic electron transfer in photosystem II complex is discussed.     

Evidence for a role of raffinose in stabilizing photosystem II during freeze–thaw cycles

A role of non-reducing sugars like sucrose and raffinose in the protection of plant cells against damage during freezing has been proposed for many species, but reports on physiological effects are conflicting. Non-aqueous fractionation of mesophyll cell compartments in Arabidopsis thaliana was used to show that sucrose and raffinose accumulate in plastids during low temperatures, pointing to a physiological role in protecting the photosynthetic apparatus. Comparing a previously described raffinose synthase (RS) mutant of A. thaliana with its corresponding wild type, accession Col-0, revealed that a lack of raffinose has no effect on electrolyte leakage from leaf cells after freeze–thaw cycles, supporting that raffinose is not essential for protecting the plasma membrane. However, in situ chlorophyll fluorescence showed that maximum quantum yield of PS II photochemistry (F _v/F _m) and other fluorescence parameters of cold acclimated leaves subjected to freeze–thaw cycles were significantly lower in the raffinose synthase mutant than in the corresponding wild type, indicating that raffinose is involved in stabilizing PS II of cold acclimated leaf cells against damage during freezing.     

Deletion of psbJ leads to accumulation of Psb27–Psb28 photosystem II complexes in Thermosynechococcus elongatus

The life cycle of Photosystem II (PSII) is embedded in a network of proteins that guides the complex through biogenesis, damage and repair. Some of these proteins, such as Psb27 and Psb28, are involved in cofactor assembly for which they are only transiently bound to the preassembled complex. In this work we isolated and analyzed PSII from a ΔpsbJ mutant of the thermophilic cyanobacterium Thermosynechococcus elongatus. From the four different PSII complexes that could be separated the most prominent one revealed a monomeric Psb27–Psb28 PSII complex with greatly diminished oxygen-evolving activity. The MALDI-ToF mass spectrometry analysis of intact low molecular weight subunits (< 10 kDa) depicted wild type PSII with the absence of PsbJ. Relative quantification of the PsbA1/PsbA3 ratio by LC-ESI mass spectrometry using ¹⁵N labeled PsbA3-specific peptides indicated the complete replacement of PsbA1 by the stress copy PsbA3 in the mutant, even under standard growth conditions (50 μmol photons m^? 2 s^? 1). This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: from Natural to Artificial.     

Inhibition of Calvin–Benson cycle suppresses the repair of photosystem II in Symbiodinium: implications for coral bleaching

Inhibition of Calvin–Benson cycle (CBC) activity by thermal stress has been hypothesized to cause photoinhibition of photosystem II (PSII) in zooxanthellae of reef-building corals and consequently lead to bleaching. This study tests whether the interruption of CBC by glycolaldehyde (GA) leads to photoinhibition and subsequent coral bleaching in Stylophora pistillata. When S. pistillata was incubated with GA, the O₂ evolution rate declined in a dose-dependent manner and the extent of photoinhibition, reflected by a decreased maximum quantum yield of PSII (F _v/F _m), was enhanced. The effect of GA on photoinhibition was similar to that of chloramphenicol (CAP), an inhibitor of protein synthesis in chloroplasts. When S. pistillata was incubated in weak light following a high-light-induced photoinhibitory treatment, the recovery of PSII from photoinhibition was suppressed in a similar manner to both GA- and CAP-treated samples. After incubation in moderate light at 26°C, S. pistillata showed a bleaching response only in presence of GA. These results suggest that coral bleaching-like responses are caused by interruption of the CBC activity in S. pistillata and are associated with accelerated photoinhibition through suppression of the protein synthesis-dependent repair of PSII but not to an increase in photodamage to PSII.     

The PsbQ′ protein affects the redox potential of the Q<Subscript>A</Subscript> in photosystem II

Red alga contains four extrinsic proteins in photosystem II (PSII), which are PsbO, PsbV, PsbU, and PsbQ′. Except for the PsbQ′, the composition is the same in cyanobacterial PSII. Reconstitution analysis of cyanobacterial PSII has shown that oxygen-evolving activity does not depend on the presence of PsbQ′. Recently, the structure of red algal PSII was elucidated. However, the role of PsbQ′ remains unknown. In this study, the function of the acceptor side of PSII was analyzed in PsbQ′-reconstituted PSII by redox titration of Q_A and thermoluminescence. The redox potential of Q_A was positively shifted when PsbQ′ was attached to the PSII. The positive shift of Q_A is thought to cause a decrease in the amount of triplet chlorophyll in PSII. On the basis of these results, we propose that PsbQ′ has a photoprotective function when irradiated with strong light.     

Enhanced thermotolerance of photosystem II in salt-adapted plants of the halophyte<Emphasis Type="Italic"> Artemisia anethifolia</Emphasis>

Thermotolerance of photosystem II (PSII) in leaves of salt-adapted Artemisia anethifolia L. plants (100–400 mM NaCl) was evaluated after exposure to heat stress (30–45°C) for 30 min. After exposure to 30°C, salt adaptation had no effects on the maximal efficiency of PSII photochemistry (F_v/F_m), the efficiency of excitation capture by open PSII centers (F_v/F_m), or the actual PSII efficiency (_PSII). After pretreatment at 40°C, there was a striking difference in the responses of F_v/F_m, F_v/F_m and _PSII to heat stress in non-salt-adapted and salt-adapted leaves. Leaves from salt-adapted plants maintained significantly higher values of F_v/F_m, F_v/F_m and _PSII than those from non-salt-adapted leaves. The differences in F_v/F_m, F_v/F_m and _PSII between non-salt-adapted and salt-adapted plants persisted for at least 12 h following heat stress. These results clearly show that thermotolerance of PSII was enhanced in salt-adapted plants. This enhanced thermotolerance was associated with an improvement in thermotolerance of the PSII reaction centers, the oxygen-evolving complexes and the light-harvesting complex. In addition, we observed that after exposure to 42.5°C for 30 min, non-salt-adapted plants showed a significant decrease in CO₂ assimilation rate while in salt-adapted plants CO₂ assimilation rate was either maintained or even increased to some extent. Given that photosynthesis is considered to be the physiological process most sensitive to high-temperature damage and that PSII appears to be the most heat-sensitive part of the photosynthetic apparatus, enhanced thermotolerance of PSII may be of significance for A. anethifolia, a halophyte plant, which grows in the high-salinity regions in the north of China, where the air temperature in the summer is often as high as 45°C.     

The acceptor side of photosystem II is damaged more severely than the donor side of photosystem II in ‘Honeycrisp’ apple leaves with zonal chlorosis

To investigate the photoinhibition of photosynthesis in ‘Honeycrisp’ apple (Malus domestica Borkh. cv. Gala) leaves with zonal chlorosis, we compared pigments, CO₂ assimilation and chlorophyll (Chl) a fluorescence (OJIP) transient between chlorotic leaves and normal ones. Chl and carotenoids (Car) contents, Chl a/b ratio, and absorptance were lower in chlorotic leaves than in normal ones, whereas Car/Chl ratio was higher in the former. Although CO₂ assimilation and stomatal conductance were lower in chlorotic leaves, intercellular CO₂ concentration did not differ significantly between the two leaf types. Compared with normal leaves, chlorotic ones had increased deactivation of oxygen-evolving complexes (OEC), minimum fluorescence (F _o), dissipated energy, relative variable fluorescence at L-, W-, J- and I-steps, and decreased maximum fluorescence (F _m), maximum quantum yield for primary photochemistry (F _v /F _m or TR_o/ABS), quantum yield for electron transport (ET_o/ABS), quantum yield for the reduction of end acceptors of photosystem I (PSI) (φ_Ro and RE_o/ABS), maximum amplitude of IP phase, amount of active photosystem II (PSII) reaction centers (RCs) per cross section (CS) and total performance index (PI_tot,abs). In conclusion, photoinhibition occurs at both the donor (i.e., the OEC) and the acceptor sides of PSII in chlorotic leaves. The acceptor side is damaged more severely than the donor side, which possibly is the consequence of over-reduction of PSII due to the slowdown of Calvin cycle. In addition to decreasing light absorptance by lowering Chl level, energy dissipation is enhanced to protect chlorotic leaves from photo-oxidative damage.     

Cryo-EM structure of monomeric photosystem II at 2.78 Å resolution reveals factors important for the formation of dimer

Photosystem II (PSII) functions mainly as a dimer to catalyze the light energy conversion and water oxidation reactions. However, monomeric PSII also exists and functions in vivo in some cases. The crystal structure of monomeric PSII has been solved at 3.6 Å resolution, but it is still not clear which factors contribute to the formation of the dimer. Here, we solved the structure of PSII monomer at a resolution of 2.78 Å using cryo-electron microscopy (cryo-EM). From our cryo-EM density map, we observed apparent differences in pigments and lipids in the monomer-monomer interface between the PSII monomer and dimer. One β-carotene and two sulfoquinovosyl diacylglycerol (SQDG) molecules are found in the monomer-monomer interface of the dimer structure but not in the present monomer structure, although some SQDG and other lipid molecules are found in the analogous region of the low-resolution crystal structure of the monomer, or cryo-EM structure of an apo-PSII monomer lacking the extrinsic proteins from Synechocystis sp. PCC 6803. In the current monomer structure, a large part of the PsbO subunit was also found to be disordered. These results indicate the importance of the β-carotene, SQDG and PsbO in formation of the PSII dimer.     

Involvement of sulfoquinovosyl diacylglycerol in the structural integrity and heat-tolerance of photosystem II

To examine the role of sulfoquinovosyl diacylglycerol (SQDG) in thylakoid membranes, we compared the structural and functional properties of photosystem II (PSII) between a mutant of Chlamydomonas reinhardtii defective in SQDG ( hf-2) and the wild type. The PSII core complex of hf-2, as compared with that of the wild type, showed structural fragility when solubilized with a detergent, dodecyl beta- d-maltoside, suggesting that the physical properties of the PSII complex were altered by the loss of SQDG. On the other hand, exposure of the cells to 41 degrees C for 120 min in the dark decreased the PSII activity to 70% and 50% of the initial levels in the wild type and hf-2, respectively, which implies that the PSII activity, in the absence of SQDG, becomes less stable under heat-stress conditions. PSII inactivated to 60% of the initial level by dark incubation at 41 degrees C was reactivated by following illumination even at 41 degrees C to more than 90% in the wild type, but only to 70% in hf-2. These results suggest that PSII inactivated by heat recovers through some mechanism dependent on light, and that SQDG participates in functioning of the mechanism. The conformational disorder of PSII caused by the defect in SQDG might be correlated with the increased susceptibility of its activity to heat-stress.     

Recovery of photosystem I and II activities during re-hydration of lichen<Emphasis Type="Italic"> Hypogymnia physodes</Emphasis> thalli

Photochemical efficiencies of photosystem I (PSI) and photosystem II (PSII) were studied in dry thalli of the lichen Hypogymnia physodes and during their re-hydration. In dry thalli, PSII reaction centers are photochemically inactive, as evidenced by the absence of variable chlorophyll (Chl) fluorescence, whereas the primary electron donor of PSI, P700, exhibits irreversible oxidation under continuous light. Upon application of multiple- and, particularly, single-turnover pulses in dry lichen, P700 oxidation partially reversed, which indicated recombination between P700⁺ and the reduced acceptor F_X of PSI. Re-wetting of air-dried H. physodes initiated the gradual restoration of reversible light-induced redox reactions in both PSII and PSI, but the recovery was faster in PSI. Two slow components of P700⁺ reduction occurred after irradiation of partially and completely hydrated thalli with strong white light. In contrast, no slow component was found in the kinetics of re-oxidation of Q_A^–, the reduced primary acceptor of PSII, after exposure of such thalli to white light. This finding indicated the inability of PSII in H. physodes to provide the reduction of the plastoquinone pool to significant levels. It is concluded that slow alternative electron transport routes may contribute to the energetics of photosynthesis to a larger extent in H. physodes than in higher plants.Abbreviations A₀ and A₁ Primary acceptor chlorophyll and secondary electron acceptor phylloquinone - Chl a Chlorophyll a - F_m Maximal level of chlorophyll fluorescence when all PSII centers are closed - F_o Minimal level of fluorescence when all PSII centers are open after dark adaptation - FR Far-red - F_v Variable fluorescence (=F_m–F_o) - F_X, F_A, and F_B Iron–sulfur centers - MT pulse Multiple-turnover pulse - PS Photosystem - P700 Reaction center chlorophyll of PSI - Q_A Primary quinone acceptor of PSII - Q_B Secondary quinone acceptor of PSII - ST pulse Single-turnover pulse     

The plastoquinol–plastoquinone exchange mechanism in photosystem II: insight from molecular dynamics simulations

In the photosystem II (PSII) of oxygenic photosynthetic organisms, the reaction center (RC) core mediates the light-induced electron transfer leading to water splitting and production of reduced plastoquinone molecules. The reduction of plastoquinone to plastoquinol lowers PSII affinity for the latter and leads to its release. However, little is known about the role of protein dynamics in this process. Here, molecular dynamics simulations of the complete PSII complex embedded in a lipid bilayer have been used to investigate the plastoquinol release mechanism. A distinct dynamic behavior of PSII in the presence of plastoquinol is observed which, coupled to changes in charge distribution and electrostatic interactions, causes disruption of the interactions seen in the PSII–plastoquinone complex and leads to the “squeezing out” of plastoquinol from the binding pocket. Displacement of plastoquinol closes the second water channel, recently described in a 2.9 Å resolution PSII structure (Guskov et al. in Nat Struct Mol Biol 16:334–342, 2009), allowing to rule out the proposed “alternating” mechanism of plastoquinol–plastoquinone exchange, while giving support to the “single-channel” one. The performed simulations indicated a pivotal role of D₁-Ser264 in modulating the dynamics of the plastoquinone binding pocket and plastoquinol–plastoquinone exchange via its interaction with D₁-His252 residue. The effects of the disruption of this hydrogen bond network on the PSII redox reactions were experimentally assessed in the D₁ site-directed mutant Ser264Lys.     

Crystal structure of the Psb28 accessory factor of Thermosynechococcus elongatus photosystem II at 2.3 Å

Members of the Psb28 family of proteins are accessory factors implicated in the assembly and repair of the photosystem II complex. We present here the crystal structure of the Psb28 protein (Tlr0493) found in the thermophilic cyanobacterium Thermosynechococcus elongatus at a resolution of 2.3 Å. Overall the crystal structure of the Psb28 monomer is similar to the solution structures of C-terminally His-tagged Psb28-1 from Synechocystis sp. PCC 6803 obtained previously by nuclear magnetic resonance spectroscopy. One new aspect is that Escherichia coli-expressed T. elongatus Psb28 is able to form dimers in solution and packs as a dimer of dimers in the crystal. Analysis of wild type and mutant strains of Synechocystis 6803 by blue native-polyacrylamide gel electrophoresis suggests that Psb28-1, the closest homologue to T. elongatus Psb28 in this organism, also exists as an oligomer in vivo, most likely a dimer. In line with the prediction based on the crystal structure of T. elongatus Psb28, the addition of a 3× Flag-tag to the C-terminus of Synechocystis 6803 Psb28-1 interferes with the accumulation of the Psb28-1 oligomer in vivo. In contrast, the more distantly related Psb28-2 protein found in Synechocystis 6803 lacks the residues that stabilize dimer formation in the T. elongatus Psb28 crystal and is detected as a monomer in vivo. Overall our data suggest that the dimer interface in the Psb28 crystal might be physiologically relevant.     

Interaction of α-tocopherol quinone, α-tocopherol and other prenyllipids with photosystem II

We have found that plastoquinone-A (PQ-A) and α-tocopherol (α-Toc) increased the reduction level of the high-potential form of cytochrome b-559 (cyt. b-559 HP) and α-tocopherol quinone (α-TQ) decreased the level of this cytochrome form in Scenedesmus obliquus wild-type, while the investigated prenyllipids were not active in the restoration of the cyt. b-559 HP form in Scenedesmus PS28 mutant and Synechococcus 6301 (Anacystis nidulans) where the cyt. b-559 HP form is naturally not present. Among the tested prenyllipids, α-TQ quenched fluorescence in thylakoids of S. obliquus wild-type, the PS28 mutant and tobacco to the highest extent, while PQ-A was less effective in this respect. α-Tocopherol showed the opposite effect to α-TQ and it was rather small. The fluorescence quenching measurements of thylakoids in the presence of DCMU (3-(3,4-dichlorophenyl)-1,1-dimethylurea) showed that the α-Toc and FCCP (carbonylcyanide-p-trifluoromethoxy-phenyl-hydrazone) did not quench non-photochemically chlorophyll fluorescence while PQ-9 and α-TQ were effective fluorescence quenchers at higher concentrations (> 15 μM). However, at the lower α-TQ concentrations where its effective fluorescence quenching was found in DCMU-free samples, there was nearly no quenching effect by α-TQ observed in DCMU-treated thylakoids. This suggested a specific, not non-photochemical, DCMU sensitive, fluorescence quenching of photosystem II (PSII) at low α-TQ concentrations which is probably connected with the cyclic electron transport around PSII and might have a function of excess light energy dissipation. The effects of α-TQ on PSII resembled those of FCCP under many respects which might suggest similar mechanism of action of these compounds on PSII, i.e. the catalytic deprotonation and/or redox changes of some components of PSII such as the water splitting system, tyrosine D, Chl_z or cytochrome b-559.     

Cytochrome b₅₅₉ and cyclic electron transfer within photosystem II

Cytochrome b??? (Cyt b???), β-carotene (Car), and chlorophyll (Chl) cofactors participate in the secondary electron-transfer pathways in photosystem II (PSII), which are believed to protect PSII from photodamage under conditions in which the primary electron-donation pathway leading to water oxidation is inhibited. Among these cofactors, Cyt b??? is preferentially photooxidized under conditions in which the primary electron-donation pathway is blocked. When Cyt b??? is preoxidized, the photooxidation of several of the 11 Car and 35 Chl molecules present per PSII is observed. In this review, the discovery of the secondary electron donors, their structures and electron-transfer properties, and progress in the characterization of the secondary electron-transfer pathways are discussed. This article is part of a Special Issue entitled: Photosystem II.     

Protection by α-tocopherol of the repair of photosystem II during photoinhibition in Synechocystis sp. PCC 6803

α-Tocopherol is a lipophilic antioxidant that is an efficient scavenger of singlet oxygen. We investigated the role of α-tocopherol in the protection of photosystem II (PSII) from photoinhibition using a mutant of the cyanobacterium Synechocystis sp. PCC 6803 that is deficient in the biosynthesis of α-tocopherol. The activity of PSII in mutant cells was more sensitive to inactivation by strong light than that in wild-type cells, indicating that lack of α-tocopherol enhances the extent of photoinhibition. However, the rate of photodamage to PSII, as measured in the presence of chloramphenicol, which blocks the repair of PSII, did not differ between the two lines of cells. By contrast, the repair of PSII from photodamage was suppressed in mutant cells. Addition of α-tocopherol to cultures of mutant cells returned the extent of photoinhibition to that in wild-type cells, without any effect on photodamage. The synthesis de novo of various proteins, including the D1 protein that plays a central role in the repair of PSII, was suppressed in mutant cells under strong light. These observations suggest that α-tocopherol promotes the repair of photodamaged PSII by protecting the synthesis de novo of the proteins that are required for recovery from inhibition by singlet oxygen.     

Is carbonic anhydrase activity of photosystem II required for its maximum electron transport rate?

It is known, that the multi-subunit complex of photosystem II (PSII) and some of its single proteins exhibit carbonic anhydrase activity. Previously, we have shown that PSII depletion of HCO₃^?/CO₂ as well as the suppression of carbonic anhydrase activity of PSII by a known inhibitor of α?carbonic anhydrases, acetazolamide (AZM), was accompanied by a decrease of electron transport rate on the PSII donor side. It was concluded that carbonic anhydrase activity was required for maximum photosynthetic activity of PSII but it was not excluded that AZM may have two independent mechanisms of action on PSII: specific and nonspecific. To investigate directly the specific influence of carbonic anhydrase inhibition on the photosynthetic activity in PSII we used another known inhibitor of α?carbonic anhydrase, trifluoromethanesulfonamide (TFMSA), which molecular structure and physicochemical properties are quite different from those of AZM. In this work, we show for the first time that TFMSA inhibits PSII carbonic anhydrase activity and decreases rates of both the photo-induced changes of chlorophyll fluorescence yield and the photosynthetic oxygen evolution. The inhibitory effect of TFMSA on PSII photosynthetic activity was revealed only in the medium depleted of HCO₃^?/CO₂. Addition of exogenous HCO₃^? or PSII electron donors led to disappearance of the TFMSA inhibitory effect on the electron transport in PSII, indicating that TFMSA inhibition site was located on the PSII donor side. These results show the specificity of TFMSA action on carbonic anhydrase and photosynthetic activities of PSII. In this work, we discuss the necessity of carbonic anhydrase activity for the maximum effectiveness of electron transport on the donor side of PSII.     

Is there a direct chloride cofactor requirement in the oxygen-evolving reactions of photosystem II?

The dark incubation at room temperature of photosystem II (PS II) membrane fragments in a chloride-free medium at pH 6.3 slowly leads to large chloride-restorable and non-restorable O₂ evolution activity losses with time as compared with control samples incubated in the presence of 10 mM NaCl. The chloride requirement in O₂ evolution generated under these conditions reveals a complex interplay among various experimental parameters, including the source of the plant material, the times of incubation, the sample concentration, the chloride concentration, as well as those treatments which are believed to specifically displace chloride from PS II such as alkaline pH pretreatment and Na₂SO₄ addition. The results indicate that secondary, structural changes within the PS II complex are an important factor in determining the influence of chloride on the O₂ evolution activity and raise the question whether or not chloride ions actually play a direct cofactor role in the water-oxidizing reactions leading to O₂ evolution.Abbreviations Chl chlorophyll - EPR electron paramagnetic resonance - MES 2-(N-morpholino) ethanesulfonic acid - NMR nuclear magnetic resonance - PS II photosystem II     

Room temperature photooxidation of β-carotene and peripheral chlorophyll in photosystem II reaction centre

Differential kinetic absorption spectra were measured during actinic illumination of photosystem II reaction centres and core complexes in the presence of electron acceptors silicomolybdate and ferricyanide. The spectra of samples with ferricyanide differ from those with both ferricyanide and silicomolybdate. Near-infrared spectra show temporary beta-carotene and peripheral chlorophyll oxidation during room temperature actinic illumination. Peripheral chlorophyll is photooxidized even after decay of beta-carotene oxidation activity and significant reduction of beta-carotene content in both reaction centres and photosystem II core complexes. Besides, new carotenoid cation is observed after about 1 s of actinic illumination in the reaction centres when silicomolybdate is present. Similar result was observed in PSII core complexes. HPLC analyses of illuminated reaction centres reveal several novel carotenoids, whereas no new carotenoid species were observed in HPLC of illuminated core complexes. Our data support the proposal that pigments of inner antenna are a sink of cations originating in the photosystem II reaction centre.     

Temperature dependence of the formation of the g ~ 5 EPR signal in the oxygen evolving complex of photosystem II

Photosynthesis Research - The temperature dependence of the formation of the g?~?5 S2 state electron paramagnetic resonance (EPR) signal in photosystem II (PSII) was investigated. The...