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BBA - Bioenergetics (v.1757, #11)

Editorial Board (pp. ii).

Commentary on: “Photosynthesis and negative entropy production�? by Jennings and coworkers by Jérôme Lavergne (pp. 1453-1459).

This commentary argues against the view that photochemical energy conversion violates the second law of thermodynamics, as expressed in a recent paper [R.C. Jennings, E. Engelmann, F. Garlaschi, A.P. Casazza, G. Zucchelli. Photosynthesis and negative entropy production. Biochim. Biophys. Acta 1709 (2005) 251-255]. The basic principles of free energy conversion by a photo-electrochemical cell are outlined, emphasizing the fact that the potential depends on the relative population of the excited state and thus on the illumination intensity.

Keywords: Photosynthesis; Thermodynamic; Energy yield; Second law; Dissipation; Carnot; Entropy; Photochemical energy conversion; Solar energy conversion

Reply to “Commentary on Photosynthesis and Negative Entropy Production by Jennings and coworkers�? by J. Lavergne by R.C. Jennings; A.P. Casazza; E. Belgio; F.M. Garlaschi; G. Zucchelli (pp. 1460-1462).

It is argued that the chemical potential analogy does not provide useful information on the thermodynamics of photosystems, as the thermodynamic efficiency of an absorbed quantum is not considered. Instead, the approach based on either entropy balance or entropy flux considerations does provide this information. At high thermodynamic efficiencies, primary photochemistry can, in principle, violate the Second Law of Thermodynamics.

Keywords: Photosynthesis; Entropy; Photochemistry

Cold acclimation and oxygen consumption in the thymus by Clare M. Brennan; Eamon P. Breen; Richard K. Porter (pp. 1463-1468).

Mitochondrial uncoupling protein 1 is usually associated with brown adipose tissue but has recently been discovered in rat and mouse thymus. We wished to establish whether there was a thermogenic role for UCP 1 in thymus and thus examined the effect of 5 weeks cold-acclimation on rat thymus tissue abundance, thymocyte oxygen consumption, thymus mitochondrial abundance, uncoupling protein 1 expression and function. We found that thymocytes from cold-acclimated rats had oxygen consumption rates 8 times less than those from rats held at room temperature and that thymocytes from cold-acclimated rats or rats kept at room temperature were noradrenaline insensitive. In addition, we found that thymus tissue or mitochondrial abundance was not increased after cold-acclimation. However uncoupling protein 1 expression per unit mass of mitochondria was increased after cold-acclimation, as determined by immunoblotting (∼1.7-fold) and GDP binding (∼1.5-fold). Consistent with our protein expression data, we also observed an increased, state 4 (∼1.5-fold), GDP-inhibitable (∼1.3-fold) and palmitate activatable (∼1.6-fold) oxygen consumption rates in isolated thymus mitochondria. However, extrapolation of our data showed that cold-acclimation only increased the amount of UCP 1 per gram of thymus tissue ∼1.2-fold. Taken together, we conclude that UCP 1 does not have a thermogenic role in thymus.

Keywords: Abbreviations; ATP; adenosine diphosphate; B; _MAX; maximum binding capacity; BAT; brown adipose tissue; BSA; bovine serum albumin; DNP; 2,4-dinitrophenol; ECL; enhanced chemiluminescence; EDTA; ethylenediaminetetraacetic acid; EGTA; ethylene glycol-bis(β-aminoethyl ether); N,N,N′,N′; -tetraacetic acid; F; ₁; β; the β subunit of the F; ₁; fraction of the ATP synthase; FBS; foetal bovine serum; GDP; guanosine diphosphate; HEPES; (; N; -(2-hydroxyethyl)piperazine-; N′; -(2-ethanesulfonic acid)); K; _D; ligand binding affinity; PVDF; polyvinyldifluoride; ROS; reactive oxygen containing species; RPMI; Roswell Park Memorial Institute; SEM; standard error of the mean; UCP; uncoupling proteinUncoupling protein-1; Thymus; Thymocyte; Mitochondria; Purine nucleotide; Oxygen consumption

Structural characterization of NDH-1 complexes of Thermosynechococcus elongatus by single particle electron microscopy by Ana A. Arteni; Pengpeng Zhang; Natalia Battchikova; Teruo Ogawa; Eva-Mari Aro; Egbert J. Boekema (pp. 1469-1475).

The structure of the multifunctional NAD(P)H dehydrogenase type 1 (NDH-1) complexes from cyanobacteria was investigated by growing the wild type and specific ndh His-tag mutants of Thermosynechococcus elongatus BP-1 under different CO₂ conditions, followed by an electron microscopy (EM) analysis of their purified membrane protein complexes. Single particle averaging showed that the complete NDH-1 complex (NDH-1L) is L-shaped, with a relatively short hydrophilic arm. Two smaller complexes were observed, differing only at the tip of the membrane-embedded arm. The smallest one is considered to be similar to NDH-1M, lacking the NdhD1 and NdhF1 subunits. The other fragment, named NDH-1I, is intermediate between NDH-1L and NDH-1M and only lacks a mass compatible with the size of the NdhF1 subunit. Both smaller complexes were observed under low- and high-CO₂ growth conditions, but were much more abundant under the latter conditions. EM characterization of cyanobacterial NDH-1 further showed small numbers of NDH-1 complexes with additional masses. One type of particle has a much longer peripheral arm, similar to the one of NADH: ubiquinone oxidoreductase (complex I) in E. coli and other organisms. This indicates that Thermosynechococcus elongatus must have protein(s) which are structurally homologous to the E. coli NuoE, -F, and -G subunits. Another low-abundance type of particle (NDH-1U) has a second labile hydrophilic arm at the tip of the membrane-embedded arm. This U-shaped particle has not been observed before by EM in a NDH-I preparation.

Keywords: NDH-1; Complex I; Thermosynechococcus elongatus; Electron microscopy

Characterization of the second external alternative dehydrogenase from mitochondria of the respiratory yeast Kluyveromyces lactis by Nuria Tarrío; M. Esperanza Cerdán; M. Isabel González Siso (pp. 1476-1484).

The mitochondria of the respiratory yeast Kluyveromyces lactis are able to reoxidize cytosolic NADPH. Previously, we characterized an external alternative dehydrogenase, KlNde1p, having this activity. We now characterize the second external alternative dehydrogenase of K. lactis mitochondria, KlNde2p. We examined its role in cytosolic NADPH reoxidation by studying heterologous expression of KlNDE2 in Saccharomyces cerevisiae mutants and by constructing Δ klnde1 and Δ klnde2 mutants. KlNde2p uses NADH or NADPH as substrates, its activity in isolated mitochondria is not regulated by exogenously added calcium and it is not down-regulated when the cells grow in glucose versus lactate. KlNde2p shows lower affinity for NADPH than KlNde1p. Both enzymes show similar pH optimum.

Keywords: Mitochondria; External alternative dehydrogenase; Respirofermentative metabolism; Kluyveromyces; NADPHl; KlNDE2

The metal-binding sites of the zinc-transporting P-type ATPase of Escherichia coli. Lys⁶⁹³ and Asp⁷¹⁴ in the seventh and eighth transmembrane segments of ZntA contribute to the coupling of metal binding and ATPase activity by Juha Okkeri; Tuomas Haltia (pp. 1485-1495).

ZntA is a P-type ATPase which transports Zn²⁺, Pb²⁺ and Cd²⁺ out of the cell. Two cysteine-containing motifs, CAAC near the N-terminus and CPC in transmembrane helix 6, are involved in binding of the translocated metal. We have studied these motifs by mutating the cysteines to serines. The roles of two other possible metal-binding residues, K⁶⁹³ and D⁷¹⁴, in transmembrane helices 7 and 8, were also addressed. The mutation CAAC→SAAS reduces the ATPase activity by 50%. The SAAS mutant is phosphorylated with ATP almost as efficiently as the wild type. However, its phosphorylation with P_i is poorer than that of the wild type and its dephosphorylation rate is faster than that of the wild type ATPase. The CPC→SPS mutant is inactive but residual phosphorylation with ATP could still be observed. The most important findings of this work deal with the prospective metal-binding residues K⁶⁹³ and D⁷¹⁴: the substitution K693N eliminates the Zn²⁺-stimulated ATPase activity completely, although significant Zn²⁺-dependent phosphorylation by ATP remains. The K693N ATPase is hyperphosphorylated by P_i. ZntA carrying the change D714M has strong metal-independent ATPase activity and is very weakly phosphorylated both by ATP and P_i. In conclusion, K⁶⁹³ and D⁷¹⁴ are functionally essential and appear to contribute to the metal specificity of ZntA, most probably by being parts of the metal-binding site made up by the CPC motif.

Keywords: Abbreviations; EDTA; ethylenediaminetetraacetic acid; IPTG; isopropyl-β-; d; -thiogalactoside; P; _i; inorganic phosphate; PMSF; phenylmethylsulfonyl fluoride; TCA; trichloroacetic acid; TM; transmembrane; Tris; tris(hydroxymethyl)aminomethane; wt; wild typeP-type ATPases; Membrane protein; Metal binding site; Ion pump; Zinc; Copper

Oxygen reduction in chloroplast thylakoids results in production of hydrogen peroxide inside the membrane by Maria Mubarakshina; Sergey Khorobrykh; Boris Ivanov (pp. 1496-1503).

Hydrogen peroxide production in isolated pea thylakoids was studied in the presence of cytochrome c to prevent disproportionation of superoxide radicals outside of the thylakoid membranes. The comparison of cytochrome c reduction with accompanying oxygen uptake revealed that hydrogen peroxide was produced within the thylakoid. The proportion of electrons from water oxidation participating in this hydrogen peroxide production increased with increasing light intensity, and at a light intensity of 630 μmol quanta m−² s−¹ it reached 60% of all electrons entering the electron transport chain. Neither the presence of a superoxide dismutase inhibitor, potassium cyanide or sodium azide, in the thylakoid suspension, nor unstacking of the thylakoids appreciably affected the partitioning of electrons to hydrogen peroxide production. Also, osmolarity-induced changes in the thylakoid lumen volume, as well as variation of the lumen pH induced by the presence of Gramicidin D, had negligible effects on such partitioning. The flow of electrons participating in lumen hydrogen peroxide production was found to be near 10% of the total electron flow from water. It is concluded that a considerable amount of hydrogen peroxide is generated inside thylakoid membranes, and a possible mechanism, as well as the significance, of this process are discussed.

Keywords: Abbreviations; Chl; chlorophyll; cyt; c; cytochrome; c; Gr D; gramicidin D; PETC; photosynthetic electron transport chain; PQ; plastoquinone; PQH; ^·; plastosemiquinone; PQH; ₂; plastohydroquinone, plastoquinol; PSI; photosystem I; PSII; photosystem II; ROS; reactive oxygen species; SOD; superoxide dismutasePhotoreduction of oxygen; Hydrogen peroxide; Thylakoids; Membrane

Xanthophyll-induced aggregation of LHCII as a switch between light-harvesting and energy dissipation systems by Wieslaw I. Gruszecki; Wojciech Grudzinski; Małgorzata Gospodarek; Magdalena Patyra; Waldemar Maksymiec (pp. 1504-1511).

The xanthophyll cycle pigments, violaxanthin and zeaxanthin, present outside the light-harvesting pigment–protein complexes of Photosystem II (LHCII) considerably enhance specific aggregation of proteins as revealed by analysis of the 77 K chlorophyll a fluorescence emission spectra. Analysis of the infrared absorption spectra in the Amide I region shows that the aggregation is associated with formation of intermolecular hydrogen bonding between the α helices of neighboring complexes. The aggregation gives rise to new electronic energy levels, in the Soret region (530 nm) and corresponding to the Q spectral region (691 nm), as revealed by analysis of the resonance light scattering spectra. New electronic energy levels are interpreted in terms of exciton coupling of protein-bound photosynthetic pigments. The energy of the Q excitonic level of chlorophyll is not high enough to drive the light reactions of Photosystem II but better suited to transfer excitation energy to Photosystem I, which creates favourable energetic conditions for the state I–state II transition. The lack of fluorescence emission from this energy level, at physiological temperatures, is indicative of either very high thermal energy conversion rate or efficient excitation quenching by carotenoids. Chlorophyll a fluorescence was quenched up to 61% and 34% in the zeaxanthin- and violaxanthin-containing samples, respectively, as compared to pure LHCII. Enhanced aggregation of LHCII, observed in the presence of the xanthophyll cycle pigments, is discussed in terms of the switch between light-harvesting and energy dissipation systems.

Keywords: Carotenoid; LHCII; Photoprotection; Protein aggregation; Xanthophyll cycle; Violaxanthin; Zeaxanthin

The state transition mechanism—simply depending on light-on and -off in Spirulina platensis by Heng Li; Donghui Li; Shuzhen Yang; Jie Xie; Jingquan Zhao (pp. 1512-1519).

The state transition in cyanobacteria is a long-discussed topic of how the photosynthetic machine regulates the excitation energy distribution in balance between the two photosystems. In the current work, whether the state transition is realized by “mobile phycobilisome (PBS)�? or “energy spillover�? has been clearly answered by monitoring the spectral responses of the intact cells of the cyanobacterium Spirulina platensis. Firstly, light-induced state transition depends completely on a movement of PBSs toward PSI or PSII while the redox-induced one on not only the “mobile PBS�? but also an “energy spillover�?. Secondly, the “energy spillover�? is triggered by dissociation of PSI trimers into the monomers which specially occurs under a case from light to dark, while the PSI monomers will re-aggregate into the trimers under a case from dark to light, i.e., the PSI oligomerization is reversibly regulated by light switch on and off. Thirdly, PSI oligomerization is regulated by the local H⁺ concentration on the cytosol side of the thylakoid membranes, which in turn is regulated by light switch on and off. Fourthly, PSI oligomerization change is the only mechanism for the “energy spillover�?. Thus, it can be concluded that the “mobile PBS�? is a common rule for light-induced state transition while the “energy spillover�? is only a special case when dark condition is involved.

Keywords: Abbreviations; APC; Allophycocynin; Chl; chlorophyll; C-PC; C-phycocyanin; DCMU; 3-(3, 4-dichlorophenyl)-1, 1-dimethylurea; HEPES; 2-[4-(2-hydroxyethyl)-1-piperazinyl] ethanesulfonic acid; PSI; photosystem I; PSII; photosystem II; PBS; phycobilisomeEnergy spillover; Mobile phycobilisome; Oligomerization; Photosystem I; Photosystem II; State transition

Kinetic study of the plastoquinone pool availability correlated with H₂O₂ release in seawater and antioxidant responses in the red alga Kappaphycus alvarezii exposed to single or combined high light, chilling and chemical stresses by Marcelo P. Barros; Orlando Necchi Jr.; Pio Colepicolo; Marianne Pedersén (pp. 1520-1528).

Under biotic/abiotic stresses, the red alga Kappaphycus alvarezii reportedly releases massive amounts of H₂O₂ into the surrounding seawater. As an essential redox signal, the role of chloroplast-originated H₂O₂ in the orchestration of overall antioxidant responses in algal species has thus been questioned. This work purported to study the kinetic decay profiles of the redox-sensitive plastoquinone pool correlated to H₂O₂ release in seawater, parameters of oxidative lesions and antioxidant enzyme activities in the red alga Kappaphycus alvarezii under the single or combined effects of high light, low temperature, and sub-lethal doses of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) and 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB), which are inhibitors of the thylakoid electron transport system. Within 24 h, high light and chilling stresses distinctly affected the availability of the PQ pool for photosynthesis, following Gaussian and exponential kinetic profiles, respectively, whereas combined stimuli were mostly reflected in exponential decays. No significant correlation was found in a comparison of the PQ pool levels after 24 h with either catalase (CAT) or ascorbate peroxidase (APX) activities, although the H₂O₂ concentration in seawater ( R=0.673), total superoxide dismutase activity ( R=0.689), and particularly indexes of protein ( R=0.869) and lipid oxidation ( R=0.864), were moderately correlated. These data suggest that the release of H₂O₂ from plastids into seawater possibly impaired efficient and immediate responses of pivotal H₂O₂-scavenging activities of CAT and APX in the red alga K. alvarezii, culminating in short-term exacerbated levels of protein and lipid oxidation. These facts provided a molecular basis for the recognized limited resistance of the red alga K. alvarezii under unfavorable conditions, especially under chilling stress.

Keywords: Abbreviations; APX; ascorbate peroxidase; ASW; artificial seawater; CAT; catalase; CD; conjugated dienes; CHL a; chlorophyll a; DCMU; 3-(3,4-dichlorophenyl)-1,1-dimethylurea; DBMIB; 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone; DTNB; 5,5′-dithio-; bis; (2-nitrobenzoic acid); F; ₀; basal fluorescence of a dark-acclimated alga; F; _m; maximal fluorescence of a dark-acclimated alga; FW; fresh weight; GSH; glutathione; HL; high light treatment; LL; low light treatment; PAR; photosynthesizing active radiation; PQ pool; plastoquinone pool; PQH; ₂; reduced plastoquinone; PS I; photosystem I; PS II; photosystem II; ROS; reactive oxygen species; SOD; superoxide dismutase; TBARS; thiobarbituric acid reactive substancesPlastoquinone pool; Hydrogen peroxide; Alga; Oxidative stress; Antioxidant; Kappaphycus alvarezii

Assignment of a kinetic component to electron transfer between iron–sulfur clusters F_X and F_A/B of Photosystem I by Martin Byrdin; Stefano Santabarbara; Feifei Gu; Wendy V. Fairclough; Peter Heathcote; Kevin Redding; Fabrice Rappaport (pp. 1529-1538).

We studied the kinetics of reoxidation of the phylloquinones in Chlamydomonas reinhardtii Photosystem I using site-directed mutations in the PhQ_A-binding site and of the residues serving as the axial ligand to ec3_A and ec3_B chlorophylls. In wild type PS I, these kinetics are biphasic, and mutations in the binding region of PhQ_A induced a specific slowing down of the slow component. This slowing allowed detection of a previously unobserved 180-ns phase having spectral characteristics that differ from electron transfer between phylloquinones and F_X. The new kinetic phase thus reflects a different reaction that we ascribe to oxidation of F_X⁻ by the F_A/B FeS clusters. These absorption changes partly account for the differences between the spectra associated with the two kinetic components assigned to phylloquinone reoxidation. In the mutant in which the axial ligand to ec3_A (PsaA–Met688) was targeted, about 25% of charge separations ended in P₇₀₀⁺A₀⁻ charge recombination; no such recombination was detected in the B-side symmetric mutant. Despite significant changes in the amplitude of the components ascribed to phylloquinone reoxidation in the two mutants, the overall nanosecond absorption changes were similar to the wild type. This suggests that these absorption changes are similar for the two different phylloquinones and that part of the differences between the decay-associated spectra of the two components reflect a contribution from different electron acceptors, i.e. from an inter-FeS cluster electron transfer.

Keywords: Abbreviations; A; ₀; (A; ₀; –); primary electron acceptor in PS I (a chlorophyll a) in the oxidized (reduced) state; A; ₁; (A; ₁; –); secondary electron acceptor in PS I (a phylloquinone) in the oxidized (reduced) state; Chl; a; chlorophyll; a; Chl a′; C-13 epimer of Chl; a; DAS; decay associated spectrum spectra; ET; electron transfer; FeS; iron–sulfur cluster; F; _X; , F; _A; and F; _B; three [4Fe–4S] clusters in PS I; P; ₇₀₀; (P; ₇₀₀; ⁺; ); primary electron donor of PS I in the reduced (oxidized) state; PhQ; phylloquinone; PS I; photosystem I; WT; wild-type control strain

Acclimation of mesophyll and bundle sheath chloroplasts of maize to different irradiances during growth by Anna Drozak; Elżbieta Romanowska (pp. 1539-1546).

The regulation by light of the photosynthetic apparatus, and composition of light-harvesting complexes in mesophyll and bundle sheath chloroplasts was investigated in maize. Leaf chlorophyll content, level of plastoquinone, PSI and PSII activities and Lhc polypeptide compositions were determined in plants grown under high, moderate and low irradiances. Photochemical efficiency of PSII, photochemical fluorescence quenching and non-photochemical fluorescence quenching over a range of actinic irradiances were also determined, using chlorophyll a fluorescence analysis. Acclimation of plants to different light conditions caused marked changes in light-harvesting complexes, LHCI and LHCII, and antenna complexes were also reorganized in these types of chloroplasts. The level of LHCII increased in plants grown in low light, even in agranal bundle sheath chloroplasts where the amount of PSII was strongly reduced. Irradiance also affected LHCI complex and the number of structural polypeptides, in this complex, generally decreased in chloroplasts from plants grown under lower light. Surprisingly moderate and low irradiances during growth do not affect the light reaction and fluorescence parameters of plants but generated differences in composition of light-harvesting complexes in chloroplasts. On the other hand, the changes in photosynthetic apparatus in plants acclimated to high light, resulted in a higher efficiency of photosynthesis. Based on these observations we propose that light acclimation to high light in maize is tightly coordinated adjustment of light reaction components/activity in both mesophyll and bundle sheath chloroplasts. Acclimation is concerned with balancing light utilization and level of the content of LHC complexes differently in both types of chloroplasts.

Keywords: Bundle sheath; Electron transport; Light acclimation; Light-harvesting complexes; Maize; Mesophyll; PhotosystemAbbreviations; BS; bundle sheath; Chl; chlorophyll; DCPIP; 2,6-dichlorophenolindophenol; DCMU; 3-(3,4-dichlorophenyl)-1,1-dimethylurea; HL; ML and LL, high-, moderate- and low-light; LHCI and LHCII; light-harvesting complexes of photosystem I, and II; M; mesophyll; MV; methyl viologen; PPFD; photosynthetic photon flux density; PQ; plastoquinone; PSI and PSII; photosystem I and II; PVDF; polyvinylidine difluoride; SDS PAGE; polyacrylamide gel electrophoresis in presence of SDS; TMPD; tetramethyl-p-phenylenediamine

Interaction of N,N,N′,N′-tetramethyl- p-phenylenediamine with photosystem II as revealed by thermoluminescence: Reduction of the higher oxidation states of the Mn cluster and displacement of plastoquinone from the Q_B niche by Alain Gauthier; Sridharan Govindachary; Johanne Harnois; Robert Carpentier (pp. 1547-1556).

The flash-induced thermoluminescence (TL) technique was used to investigate the action of N,N,N′,N′-tetramethyl- p-phenylenediamine (TMPD) on charge recombination in photosystem II (PSII). Addition of low concentrations (μM range) of TMPD to thylakoid samples strongly decreased the yield of TL emanating from S₂Q_B⁻ and S₃Q_B⁻ (B-band), S₂Q_A⁻ (Q-band), and Y_D⁺Q_A⁻ (C-band) charge pairs. Further, the temperature-dependent decline in the amplitude of chlorophyll fluorescence after a flash of white light was strongly retarded by TMPD when measured in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU). Though the period-four oscillation of the B-band emission was conserved in samples treated with TMPD, the flash-dependent yields (Y_n) were strongly declined. This coincided with an upshift in the maximum yield of the B-band in the period-four oscillation to the next flash. The above characteristics were similar to the action of the ADRY agent, carbonylcyanide m-chlorophenylhydrazone (CCCP). Simulation of the B-band oscillation pattern using the integrated Joliot–Kok model of the S-state transitions and binary oscillations of Q_B confirmed that TMPD decreased the initial population of PSII centers with an oxidized plastoquinone molecule in the Q_B niche. It was deduced that the action of TMPD was similar to CCCP, TMPD being able to compete with plastoquinone for binding at the Q_B-site and to reduce the higher S-states of the Mn cluster.

Keywords: Abbreviations; ADRY; accelerator of the deactivation reactions; CCCP; carbonylcyanide m-chlorophenylhydrazone; Chl; chlorophyll; DCMU; 3-(3,4-dichlorophenyl)-1,1-dimethylurea; FCCP; carbonylcyanide; p; -(trifluromethoxy)-phenylhydrazone; F; _v; variable fluorescence; OEC; oxygen evolving complex; P680; the primary electron donor of photosystem II; Pheo; Pheophytin (the primary electron acceptor of PSII); PS; photosystem; PQ; plastoquinone; Q; _A; and Q; _B; primary and secondary quinone acceptors of photosystem II; RC; reaction center; TMPD; N,N,N′,N′; -tetramethyl-; p; -phenylenediamine; TL; thermoluminescence; T; _m; temperature maximum of thermoluminescence emission; Y; _D; the redox active tyrosine 160 of D2 protein; Y; _z; the redox active tyrosine 161 of D1 subunitThylakoid membrane; Photosystem; Charge recombination; Manganese cluster; Plastoquinone; Thermoluminescence

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BBA - Bioenergetics (v.1757, #11)