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Accueil > Départements > Biochimie, Biophysique et Biologie Structurale > Alain BOUSSAC : Photosystème II

Photosystème II

Publications de l’équipe

2019


  • A. Boussac, « Temperature dependence of the high-spin S-2 to S-3 transition in Photosystem II: Mechanistic consequences », Biochimica Et Biophysica Acta-Bioenergetics, vol. 1860, nᵒ 6, p. 508-518, juin 2019.
    Résumé : The Mn4CaO5-cluster in Photosystem II advances through five oxidation states, S-0 to S-4, before water is oxidized and O-2 is generated. The S-2-state exhibits either a low-spin, S = 1/2 (S-2(LS)), or a high-spin state, S = 5/2 (S-2(HS)). Increasing the pH favors the S-2(HS) Sens configuration and mimics the formation of Tyr(z)center dot in the S-2(LS)-state at lower pH values (Boussac et al. Biochim. Biophys. Acta 1859 (2018) 342). Here, the temperature dependence of the S-2(HS) to S-3 transition was studied by EPR spectroscopy at pH 8.6. The present data strengthened the involvement of S2I Us as a transient state in the S(2)(LS)Tyr(z)center dot S(2)(HS)Tyr(z) -> S(3)Tyr(z) transition. Depending on the temperature, the S-2(HS) progresses to S-3 states exhibiting different EPR properties. One S-3-state with a S = 3 signal, supposed to have a structure with the water molecule normally inserted in S-2 to S-3 transition, can be formed at temperatures as low as 77 K. This suggests that this water molecule is already bound in the S-2(HS) state at pH 8.6. The nature of the EPR invisible S-3 state, formed down to 4.2 K from a S-2(HS) is state, and that of the EPR detectable S3 state formed down to 77 K are discussed. It is proposed that in the S-2(LS) to S-3 transition, at pH < 8.6, the proton release (Sugiura et al. Biochim. Biophys. Acta 1859 (2018) 1259), the S-2(LS) to S-2(HS) conversion and the binding of the water molecule are all triggered by the formation of Tyr(z)center dot.
    Mots-clés : active-site, B3S, bond formation, camn4o5 cluster, electron-paramagnetic-res, EPR, Mn(4)CaO(5) cluster, Mn4CaO5 cluster, Oxygen evolution, Photosystem II, PS2, Spin state.

  • J. - H. Chen, L. - J. Yu, A. Boussac, Z. - Y. Wang-Otomo, T. Kuang, et J. - R. Shen, « Properties and structure of a low-potential, penta-heme cytochrome c(552) from a thermophilic purple sulfur photosynthetic bacterium Thermochromatium tepidum », Photosynthesis Research, vol. 139, nᵒ 1-3, p. 281-293, mars 2019.
    Résumé : The thermophilic purple sulfur bacterium Thermochromatium tepidum possesses four main water-soluble redox proteins involved in the electron transfer behavior. Crystal structures have been reported for three of them: a high potential iron-sulfur protein, cytochrome c, and one of two low-potential cytochrome c(552) (which is a flavocytochrome c) have been determined. In this study, we purified another low-potential cytochrome c(552) (LPC), determined its N-terminal amino acid sequence and the whole gene sequence, characterized it with absorption and electron paramagnetic spectroscopy, and solved its high-resolution crystal structure. This novel cytochrome was found to contain five c-type hemes. The overall fold of LPC consists of two distinct domains, one is the five heme-containing domain and the other one is an Ig-like domain. This provides a representative example for the structures of multiheme cytochromes containing an odd number of hemes, although the structures of multiheme cytochromes with an even number of hemes are frequently seen in the PDB database. Comparison of the sequence and structure of LPC with other proteins in the databases revealed several characteristic features which may be important for its functioning. Based on the results obtained, we discuss the possible intracellular function of this LPC in Tch. tepidum.
    Mots-clés : angstrom resolution, B3S, c nitrite reductase, c554, conservation, Crystal structure, crystal-structure, Cytochrome c, Electron transfer, environment, genes, Multiheme, proteins, PS2, Purple sulfur bacteria, spectroscopy, subunit, Thermochromatium tepidum.

  • T. Motomura, L. Zuccarello, P. Sétif, A. Boussac, Y. Umena, D. Lemaire, J. N. Tripathy, M. Sugiura, R. Hienerwadel, J. - R. Shen, et C. Berthomieu, « An alternative plant-like cyanobacterial ferredoxin with unprecedented structural and functional properties: Ferredoxin with low Em discriminating against FNR », Biochimica Et Biophysica Acta. Bioenergetics, p. 148084, sept. 2019.
    Résumé : Photosynthetic [2Fe-2S] plant-type ferredoxins have a central role in electron transfer between the photosynthetic chain and various metabolic pathways. Several genes are coding for [2Fe2S] ferredoxins in cyanobacteria, with four in the thermophilic cyanobacterium Thermosynechococcus elongatus. The structure and functional properties of the major ferredoxin Fd1 are well known but data on the other ferredoxins are scarce. We report the structural and functional properties of a novel minor type ferredoxin, Fd2 of T. elongatus, homologous to Fed4 from Synechocystis sp. PCC 6803. Remarkably, the midpoint potential of Fd2, Em = -440 mV, is lower than that of Fd1, Em = -372 mV. However, while Fd2 can efficiently react with photosystem I or nitrite reductase, time-resolved spectroscopy shows that Fd2 has a very low capacity to reduce ferredoxin-NADP+ oxidoreductase (FNR). These unique Fd2 properties are discussed in relation with its structure, solved at 1.38 Å resolution. The Fd2 structure significantly differs from other known ferredoxins structures in loop 2, N-terminal region, hydrogen bonding networks and surface charge distributions. UV-Vis, EPR, and Mid- and Far-IR data also show that the electronic properties of the [2Fe2S] cluster of Fd2 and its interaction with the protein differ from those of Fd1 both in the oxidized and reduced states. The structural analysis allows to propose that valine in the motif Cys53ValAsnCys56 of Fd2 and the specific orientation of Phe72, explain the electron transfer properties of Fd2. Strikingly, the nature of these residues correlates with different phylogenetic groups of cyanobacterial Fds. With its low redox potential and its discrimination against FNR, Fd2 exhibits a unique capacity to direct efficiently photosynthetic electrons to metabolic pathways not dependent on FNR.
    Mots-clés : Alternative ferredoxin, B3S, Far-infrared of iron‑sulfur center, MROP, Photosynthetic electron transfer, PS2, Spectro-electrochemistry, UV–vis kinetics, X-ray structure.

  • M. Nakamura, A. Boussac, et M. Sugiura, « Consequences of structural modifications in cytochrome b(559) on the electron acceptor side of Photosystem II », Photosynthesis Research, vol. 139, nᵒ 1-3, p. 475-486, mars 2019.
    Résumé : Cytb(559) in Photosystem II is a heterodimeric b-type cytochrome. The subunits, PsbE and PsbF, consist each in a membrane -helix. Mutants were previously designed and studied in Thermosynechococcus elongatus (Sugiura et al., Biochim Biophys Acta 1847:276-285, 2015) either in which an axial histidine ligand of the haem-iron was substituted for a methionine, the PsbE/H23M mutant in which the haem was lacking, or in which the haem environment was modified, the PsbE/Y19F and PsbE/T26P mutants. All these mutants remained active showing that the haem has no structural role provided that PsbE and PsbF subunits are present. Here, we have carried on the characterization of these mutants. The following results were obtained: (i) the Y19F mutation hardly affect the E-m of Cytb(559), whereas the T26P mutation converts the haem into a form with a E-m much below 0mV (so low that it is likely not reducible by Q(B)(-)) even in an active enzyme; (ii) in the PsbE/H23M mutant, and to a less extent in PsbE/T26P mutant, the electron transfer efficiency from Q(A)(-) to Q(B) is decreased; (iii) the lower E-m of the Q(A)/Q(A)(-) couple in the PsbE/H23M mutant correlates with a higher production of singlet oxygen; (iv) the superoxide and/or hydroperoxide formation was not increased in the PsbE/H23M mutant lacking the haem, whereas it was significantly larger in the PsbE/T26P. These data are discussed in view of the literature to discriminate between structural and redox roles for the haem of Cytb(559) in the production of reactive oxygen species.
    Mots-clés : Acceptor side, alpha-subunit, axial-ligands, B3S, b559, Cytb 559, Cytb(559), energetics, Haem axial ligand, Photosystem II, PS2, Redox, redox properties, singlet oxygen production, site-directed mutagenesis, synechocystis pcc 6803, thermosynechococcus-elongatus, water oxidation.

  • P. Sétif, A. Boussac, et A. Krieger-Liszkay, « Near-infrared in vitro measurements of photosystem I cofactors and electron-transfer partners with a recently developed spectrophotometer », Photosynthesis Research, sept. 2019.
    Résumé : A kinetic-LED-array-spectrophotometer (Klas) was recently developed for measuring in vivo redox changes of P700, plastocyanin (PCy), and ferredoxin (Fd) in the near-infrared (NIR). This spectrophotometer is used in the present work for in vitro light-induced measurements with various combinations of photosystem I (PSI) from tobacco and two different cyanobacteria, spinach plastocyanin, cyanobacterial cytochrome c6 (cyt. c6), and Fd. It is shown that cyt. c6 oxidation contributes to the NIR absorption changes. The reduction of (FAFB), the terminal electron acceptor of PSI, was also observed and the shape of the (FAFB) NIR difference spectrum is similar to that of Fd. The NIR difference spectra of the electron-transfer cofactors were compared between different organisms and to those previously measured in vivo, whereas the relative absorption coefficients of all cofactors were determined by using single PSI turnover conditions. Thus, the (840 nm minus 965 nm) extinction coefficients of the light-induced species (oxidized minus reduced for PC and cyt. c6, reduced minus oxidized for (FAFB), and Fd) were determined with values of 0.207 ± 0.004, - 0.033 ± 0.006, - 0.036 ± 0.008, and - 0.021 ± 0.005 for PCy, cyt. c6, (FAFB) (single reduction), and Fd, respectively, by taking a reference value of + 1 for P700+. The fact that the NIR P700 coefficient is larger than that of PCy and much larger than that of other contributing species, combined with the observed variability in the NIR P700 spectral shape, emphasizes that deconvolution of NIR signals into different components requires a very precise determination of the P700 spectrum.
    Mots-clés : B3S, Cytochrome c 6, Ferredoxin, Infrared spectral deconvolution, MROP, P700, Photosystem I terminal acceptor, Plastocyanin, PS2.

  • M. Sugiura, T. Tibiletti, I. Takachi, Y. Hara, S. Kanawaku, J. Sellés, et A. Boussac, « Corrigendum to "probing the role of valine 185 of the D1 protein in the photosystem II oxygen evolution" [Biochim. Biophys. Acta Bioenerg. 1859 (2018) 1259-1273] », Biochimica Et Biophysica Acta. Bioenergetics, vol. 1860, nᵒ 3, p. 270-270, mars 2019.

  • Y. Takegawa, M. Nakamura, S. Nakamura, T. Noguchi, J. Selles, A. W. Rutherford, A. Boussac, et M. Sugiura, « New insights on Chlm function in Photosystem II from site-directed mutants of D1/T179 in Thermosynechococcus elongatus », Biochimica Et Biophysica Acta-Bioenergetics, vol. 1860, nᵒ 4, p. 297-309, avr. 2019.
    Résumé : The monomeric chlorophyll, Chl(D1), which is located between the PD1PD2 chlorophyll pair and the pheophytin, Pheo(D1), is the longest wavelength chlorophyll in the heart of Photosystem II and is thought to be the primary electron donor. Its central Mg2+ is liganded to a water molecule that is H-bonded to D1/T179. Here, two site-directed mutants, D1/T179H and D1/T179V, were made in the thermophilic cyanobacterium, Thermosynechococcus elongatus, and characterized by a range of biophysical techniques. The Mn4CaO5 cluster in the water-splitting site is fully active in both mutants. Changes in thermoluminescence indicate that i) radiative recombination occurs via the repopulation of *Chl(D1) itself; ii) non-radiative charge recombination reactions appeared to be faster in the T179H-PSII; and iii) the properties of PD1PD2 were unaffected by this mutation, and consequently iv) the immediate precursor state of the radiative excited state is the Chl(D1)(+)Pheo(D1)(-) radical pair. Chlorophyll bleaching due to high intensity illumination correlated with the amount of O-1(2) generated. Comparison of the bleaching spectra with the electrochromic shifts attributed to Chl(D1) upon Q(A)(-) formation, indicates that in the T179H-PSII and in the WT*3-PSII, the Chl(D1) itself is the chlorophyll that is first damaged by O-1(2), whereas in the T179V-PSII a more red chlorophyll is damaged, the identity of which is discussed. Thus, Chl(D1) appears to be one of the primary damage site in recombination-mediated photoinhibition. Finally, changes in the absorption of Chl(D1) very likely contribute to the well-known electrochromic shifts observed at similar to 430 nm during the S-state cycle.
    Mots-clés : B3S, charge recombination, Chl(D1), chlorophyll, core complexes, d1 subunit, Electrochromic shifts, epr signals, fluorescence, P(680), p-680, Photosystem II, primary electron-donor, PS2, Reaction center, singlet oxygen, spectroscopic properties, synechocystis-sp pcc-6803.

  • A. Vigouroux, M. Aumont-Nicaise, A. Boussac, L. Marty, L. Lo Bello, P. Legrand, K. Brillet, I. J. Schalk, et S. Moréra, « A unique ferrous iron binding mode is associated to large conformational changes for the transport protein FpvC of Pseudomonas aeruginosa », The FEBS journal, juill. 2019.
    Résumé : Pseudomonas aeruginosa secretes pyoverdine, a major siderophore to get access to iron, an essential nutrient. Pyoverdine scavenges ferric iron in the bacterial environment with the resulting complex internalized by bacteria. Iron release from pyoverdine in the periplasm involves an iron reduction by an inner membrane reductase and two solute-binding proteins (SBPs) FpvC and FpvF in association with their ABC transporter. FpvC and FpvF belong to two different subgroups of SBPs within the structural cluster A: FpvC and FpvF were proposed to be a metal-binding protein and a ferrisiderophore binding protein, respectively. Here, we report the redox state and the binding mode of iron to FpvC. We first solved the crystal structure of FpvC bound to a fortuitous Ni2+ by single anomalous dispersion method. Using a different protein purification strategy, we determined the structure of FpvC with manganese and iron, which binds to FpvC in a ferrous state as demonstrated by electron paramagnetic resonance. FpvC is the first example of a hexahistidine metal site among SBPs in which the Fe2+ redox state is stabilized under aerobic conditions. Using biophysics methods, we showed that FpvC reversibly bind a broad range of divalent ions. The structure of a mutant mimicking the apo FpvC reveals a protein in an open state with large conformational changes when compared with the metal-bound FpvC. These results highlight that the canonical metal site in FpvC is distinct from those yet described in SBPs and they provide new insights into the mechanism of PVD-Fe dissociation in P. aeruginosa. This article is protected by copyright. All rights reserved.
    Mots-clés : B3S, iron, MESB3S, PF, PIM, PS2, Pseudomonas aeruginosa, pyoverdine, siderophore, solute-binding protein.

2018


  • A. Boussac, I. Ugur, A. Marion, M. Sugiura, V. R. I. Kaila, et A. W. Rutherford, « The low spin - high spin equilibrium in the S2-state of the water oxidizing enzyme », Biochimica Et Biophysica Acta, vol. 1859, nᵒ 5, p. 342-356, févr. 2018.
    Résumé : In Photosystem II (PSII), the Mn4CaO5-cluster of the active site advances through five sequential oxidation states (S0to S4) before water is oxidized and O2is generated. Here, we have studied the transition between the low spin (LS) and high spin (HS) configurations of S2using EPR spectroscopy, quantum chemical calculations using Density Functional Theory (DFT), and time-resolved UV-visible absorption spectroscopy. The EPR experiments show that the equilibrium between S2LSand S2HSis pH dependent, with a pKa ≈ 8.3 (n ≈ 4) for the native Mn4CaO5and pKa ≈ 7.5 (n ≈ 1) for Mn4SrO5. The DFT results suggest that exchanging Ca with Sr modifies the electronic structure of several titratable groups within the active site, including groups that are not direct ligands to Ca/Sr, e.g., W1/W2, Asp61, His332 and His337. This is consistent with the complex modification of the pKaupon the Ca/Sr exchange. EPR also showed that NH3addition reversed the effect of high pH, NH3-S2LSbeing present at all pH values studied. Absorption spectroscopy indicates that NH3is no longer bound in the S3TyrZstate, consistent with EPR data showing minor or no NH3-induced modification of S3and S0. In both Ca-PSII and Sr-PSII, S2HSwas capable of advancing to S3at low temperature (198 K). This is an experimental demonstration that the S2LSis formed first and advances to S3via the S2HSstate without detectable intermediates. We discuss the nature of the changes occurring in the S2LSto S2HStransition which allow the S2HSto S3transition to occur below 200 K. This work also provides a protocol for generating S3in concentrated samples without the need for saturating flashes.
    Mots-clés : B3S, DFT, EPR, Mn(4)CaO(5) cluster, Oxygen evolution, Photosystem II, PS2, Spin state.

  • D. J. Nürnberg, J. Morton, S. Santabarbara, A. Telfer, P. Joliot, L. A. Antonaru, A. V. Ruban, T. Cardona, E. Krausz, A. Boussac, A. Fantuzzi, et A. W. Rutherford, « Photochemistry beyond the red limit in chlorophyll f-containing photosystems », Science (New York, N.Y.), vol. 360, nᵒ 6394, p. 1210-1213, 2018.
    Résumé : Photosystems I and II convert solar energy into the chemical energy that powers life. Chlorophyll a photochemistry, using red light (680 to 700 nm), is near universal and is considered to define the energy "red limit" of oxygenic photosynthesis. We present biophysical studies on the photosystems from a cyanobacterium grown in far-red light (750 nm). The few long-wavelength chlorophylls present are well resolved from each other and from the majority pigment, chlorophyll a. Charge separation in photosystem I and II uses chlorophyll f at 745 nm and chlorophyll f (or d) at 727 nm, respectively. Each photosystem has a few even longer-wavelength chlorophylls f that collect light and pass excitation energy uphill to the photochemically active pigments. These photosystems function beyond the red limit using far-red pigments in only a few key positions.
    Mots-clés : B3S, PS2.

  • M. Sugiura, T. Tibiletti, I. Takachi, Y. Hara, S. Kanawaku, J. Selles, et A. Boussac, « Probing the role of Valine 185 of the D1 protein in the Photosystem II oxygen evolution », Biochimica Et Biophysica Acta-Bioenergetics, vol. 1859, nᵒ 12, p. 1259-1273, déc. 2018.
    Résumé : In Photosystem II (PSII), the Mn4CaO5-cluster of the active site advances through five sequential oxidation states (S-0 to S-4) before water is oxidized and O-2 is generated. The V185 of the D1 protein has been shown to be an important amino acid in PSII function (Dilbeck et al. Biochemistry 52 (2013) 6824-6833). Here, we have studied its role by making a V185T site-directed mutant in the thermophilic cyanobacterium Thermosynechococcus elongatus. The properties of the V185T-PSII have been compared to those of the WT*3-PSII by using EPR spectroscopy, polarography, thermoluminescence and time-resolved UV-visible absorption spectroscopy. It is shown that the V185 and the chloride binding site very likely interact via the H-bond network linking Tyr(z) and the halide. The V185 contributes to the stabilization of S-2 into the low spin (LS), S = 1/2, configuration. Indeed, in the V185T mutant a high proportion of S-2 exhibits a high spin (HS), S = 5/2, configuration. By using bromocresol purple as a dye, a proton release was detected in the S(1)Tyr(Z)center dot -> S(2)(LS)Tyr(Z) transition in the V185T mutant in contrast to the WT*3-PSII in which there is no proton release in this transition. Instead, in WT*3-PSII, a proton release kinetically much faster than the S(2)(LS)Tyr(z)center dot -> S(3)Tyr(Z) transition was observed and we propose that it occurs in the S(2)(LS)Tyr(Z)center dot -> S(2)(HS)Tyr(Z). intermediate step before the S(2)(HS)Tyr(Z)center dot -> S(3)Tyr(Z) transition occurs. The dramatic slowdown of the S(3)Tyr(Z)center dot -> S(0)Tyr(Z) transition in the V185T mutant does not originate from a structural modification of the Mn4CaO5 cluster since the spin S = 3 S-3 EPR signal is not modified in the mutant. More probably, it is indicative of the strong implication of V185 in the tuning of an efficient relaxation processes of the H-bond network and/or of the protein.
    Mots-clés : alternating electron, B3S, charge recombination, dioxygen formation, electron-paramagnetic-res, epr signals, evolving mn4cao5 cluster, ftir difference spectroscopy, Mn4CaO5 cluster, Oxygen evolution, photosynthetic water oxidation, Photosystem II, Proton release, proton release, PS2, Spin state, thermosynechococcus-elongatus.

2016

2015

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Publications 2011-2014

-  The effect of Ca2+/Sr2+ substitution on the electronic structure of the oxygen-evolving complex of photosystem II : A combined multi-frequency EPR, 55Mn-ENDOR and DFT study of the S2 state.
Cox, N., Rapatskiy, L., Su, J.-H., Pantazis, D. A., Sugiura, M., Kulik, L., Dorlet, P., Rutherford, A. W., Neese, F., Boussac, A., Lubitz, W., Messinger, J. (2011) J. Am. Chem. Soc. 133, 3635-3648.

-  The electronic structures of the S2 states of the oxygen-evolving complexes of Photosystem II in plants and cyanobacteria in the presence and absence of methanol.
Su, J.-H., Cox, N., Ames, W., Pantazis, D. A., Rapatskiy, L., Lohmiller, T., Kulik, L. V., Dorlet, P., Rutherford, A. W., Neese, F., Boussac, A., Lubitz, W., Messinger, J. (2011) Biochim. Biophys. Acta 1807, 829–840.

-  Ca2+ determines the entropy changes associated with the formation of transition states during water oxidation by Photosystem II.
Rappaport, F., Ishida, N., Sugiura, M., Boussac, A. (2011) Energ. Environ. Sci. 4, 2520-2524.

-  The semiquinone-iron complex of Photosystem II : EPR signals assigned to the low field edge of the ground state doublet of QA•-Fe2+ and QB•-Fe2+.
Sedoud, A., Cox, N., Sugiura, M., Lubitz, W., Boussac, A. Rutherford, A. W. (2011) Biochemistry 50, 6012–6021.

-  Deactivation processes in PsbA1-Photosystem II and PsbA3-Photosystem II under photoinhibitory conditions in the cyanobacterium Thermosynechococcus elongatus.
Ogami, S., Boussac, A., Sugiura, M. (2012) Biochim. Biophys. Acta 1817, 1322–1330.

-  Environment of TyrZ in Photosystem II from Thermosynechococcus elongatus in which PsbA2 is the D1 protein.
Sugiura, M. Ogami, S., Kusumi, M., Un, S., Rappaport, F., Boussac, A. (2012) J. Biol. Chem. 287, 13336–13347.

-  Probing the role of chloride in Photosystem II from Thermosynechococcus elongatus by exchanging chloride for iodide.
Boussac, A., Ishida, N., Sugiura, M., Rappaport, F. (2012) Biochim. Biophys. Acta 1817, 802–810.

-  Influence of the PsbA1/PsbA3 and Ca2+/Sr2+ or Cl–/Br– exchanges on the redox potential of the primary quinone QA in Photosystem II as revealed by spectroelectrochemistry.
Kato, Y., Shibamoto, T., Yamamoto, S., Watanabe, T., Ishida, N., Sugiura, M., Rappaport, F., Boussac, A. (2012) Biochim. Biophys. Acta 1817, 1998–2004.

-  Detection of the Water Binding Sites of the Oxygen-evolving Complex of Photosystem II Using W-band 17O ELDOR detected NMR Spectroscopy
Rapatskiy, L., Cox, N., Savitsky, A., Ames, W. M., Sander, J., Nowacyzk, M. M. Rögner, M., Boussac, A., Neese, F., Messinger, J., Lubitz, W. (2012) J. Am. Chem. Soc 134, 16619–16634.

-  The Rotavirus Nonstructural Protein NSP5 Coordinates a [2Fe-2S] Iron-Sulfur Cluster that Modulates Interaction with RNA
Martin, D., Charpilienne, A., Parent, A., Boussac, A., D’Autreaux, B., Poupon, J., Poncet, D. (2013) FASEB J. 27, 1074–1083.

-  Charge recombination in SnTyrZ•QA−• radical pairs in D1 protein variants of Photosystem II : Long range electron transfer in the Marcus inverted region.
Boussac, A. Rappaport, F., Brettel, K., Sugiura, M. (2013) J. Phys. Chem. B 117, 3308−3314.

-  The Tll0287 protein is a hemoprotein associated with the PsbA2-Photosystem II complex in Thermosynechococcus elongatus.
Boussac, A., Koyama, K., Sugiura, M. (2013) Biochim. Biophys. Acta 1827, 1174–1182.

-  EPR characterization of the ferrous nitrosyl complex formed within the oxygenase domain of NO-synthase.
Santolini, J., Maréchal, A., Boussac, A., Dorlet, P. (2013) ChemBioChem. 14, 1852–1857.

-  Ammonia binding to the oxygen-evolving complex of Photosystem II identifies the solvent-exchangeable μ-oxo of the manganese tetramer.
Pérez Navarro, M., Ames, W. M., Nilsson, H., Lohmiller, T., Pantazis, D. A., Rapatskiy, L., Nowaczyk, M. M., Neese, F., Boussac, A., Messinger, J., Lubitz, W., Cox, C. (2013) Proc. Natl. Acad. Sci. USA 110, 15561–15566.

-  Modification of the pheophytin redox potential in Thermosynechococcus elongatus Photosystem II with PsbA3 as D1.
Sugiura, M., Azami, C., Koyama, K., Rutherford, A.W., Rappaport, F., Boussac, A. (2014) Biochim. Biophys. Acta 1837, 139–148.

-  Crystal structure at 1.5 Å resolution of the PsbV2 cytochrome from the - cyanobacterium Thermosynechococcus elongatus.
Suga, M., Lai, T.-L., Sugiura, M., Shen, J.-R., Boussac, A. (2013) FEBS Lett. 513, 3267–3272.

-  Evidence for an unprecedented histidine hydroxyl modification on D2-His336 in Photosystem II of Thermosynechoccocus vulcanus and Thermosynechoccocus elongatus.
Sugiura, M., Koyama, K., Umena, Y., Kawakami, K., Shen, J.-R., Kamiya, N., Boussac, A. (2013) Biochemistry 52, 9426–9431.

-  Some Photosystem II properties depending on the D1 protein variants in Thermosynechococcus elongatus.
Sugiura, M., Boussac, A., (2014) Biochim. Biophys. Acta 1837, 1427–1434.

-  The S2 state of the oxygen-evolving complex of Photosystem II : a combined EPR and DFT study demonstrating a general electronic structure and ligand/substrate binding.
Lohmiller, T., Krewald, V., Pérez Navarro, M., Retegan, M., Rapatskiy, L., Nowaczyk, M. M., Boussac, A., Neese, F., Lubitz, W., Pantazis, D. A., Cox, N. (2014) Phys. Chem. Chem. Phys. 16, 11877–11892.

-  Substrate-water exchange in Photosystem II is arrested prior to dioxygen formation.
Nilsson, H., Rappaport, F., Boussac, A., Messinger, J. Nature Communications. 5, 4305..

-  Electronic structure of the oxygen evolving complex in photosystem II prior to O-O bond formation
Cox, N., Retegan, M., Neese, F., Pantazis, D.A., Boussac, A., Lubitz, W. (2014) Science 345, 804-808.

-  The D1-173 amino acid is a structural determinant of the critical interaction between D1-Tyr161 (TyrZ) and D1-His190 in Photosystem II
Sugiura, M., Ozaki, Y., Nakamura, M., Cox, N., Rappaport, F., Boussac, A., (2014) Biochim. Biophys. Acta 1837, 1922–1931.

-  Assembly of oxygen-evolving Photosystem II efficiently occurs with the apo-Cytb559 but the holo-Cytb559 accelerates the recovery of a functional enzyme upon photoinhibition.
Sugiura, M., Nakamura, M., Koyama, K., Boussac, A. (2015) Biochim. Biophys. Acta sous presse.

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