Nos tutelles


Nos partenaires

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

Photosystème II

Publications de l’équipe


  • T. Motomura, M. Suga, R. Hienerwadel, A. Nakagawa, T. - L. Lai, W. Nitschke, T. Kuma, M. Sugiura, A. Boussac, et J. - R. Shen, « Crystal structure and redox properties of a novel cyanobacterial heme-protein with a His/Cys heme axial ligation and a per-arnt-sim (PAS)-like domain », The Journal of Biological Chemistry, 2017.
    Résumé : Photosystem II (PSII) catalyzes the light-induced water oxidation leading to the generation of dioxygen indispensable for sustaining aerobic life on Earth. The PSII reaction center is composed of D1 and D2 proteins encoded by the psbA and psbD genes, respectively. In cyanobacteria, different psbA genes are present in the genome. The thermophilic cyanobacterium Thermosynechococcus elongatus contains 3 psbA genes, psbA1, psbA2 and psbA3 and a new c-type heme protein, Tll0287, was found to be expressed in a strain expressing the psbA2 gene only, but the structure and function of Tll0287 are unknown. Here we solved the crystal structure of Tll0287 at a 2.0 Å resolution. The overall structure of Tll0287 was found to be similar to some kinases and sensor proteins with a per-arnt-sim (PAS)-like domain, rather than to other c-type cytochromes. The 5(th) and 6(th) axial ligands for the heme were Cys and His, instead of the His/Met or His/His ligand pairs observed for most of the c-type hemes. The redox potential, E1/2, of Tll0287 was -255 ± 20 mV versus normal hydrogen electrode at pH values above 7.5. Below this pH value, the E1/2 increased by ≈57 mV/pH unit at 15°C, suggesting the involvement of a protonatable group with a pKred = 7.2 ± 0.3. Possible functions of Tll0287 as a redox sensor under micro-aerobic conditions or a cytochrome subunit of an H2S-oxidising system, are discussed in view of the environmental conditions in which psbA2 is expressed as well as phylogenetic analysis, structural and sequence homologies.
    Mots-clés : ACTIN, B3S, cytochrome, D1 protein, Heme, His-Cys heme axial coordination, PAS domain, PAS-like domain, photosynthesis, Photosystem II, PS2, Tll0287, x-ray crystallography.



--- Exporter la sélection au format

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.

publié le , mis à jour le