Structure of photosystem II and substrate binding at room temperature.

Autor: Young ID; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Ibrahim M; Institut für Biologie, Humboldt-Universität zu Berlin, D-10099 Berlin, Germany., Chatterjee R; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Gul S; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Fuller F; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Koroidov S; Institutionen för Kemi, Kemiskt Biologiskt Centrum, Umeå Universitet, SE 90187 Umeå, Sweden., Brewster AS; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Tran R; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Alonso-Mori R; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Kroll T; Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.; SSRL, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Michels-Clark T; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Laksmono H; Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Sierra RG; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.; Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Stan CA; Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Hussein R; Institut für Biologie, Humboldt-Universität zu Berlin, D-10099 Berlin, Germany., Zhang M; Institut für Biologie, Humboldt-Universität zu Berlin, D-10099 Berlin, Germany., Douthit L; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Kubin M; Institute for Methods and Instrumentation on Synchrotron Radiation Research, Helmholtz Zentrum, 14109 Berlin, Germany., de Lichtenberg C; Institutionen för Kemi, Kemiskt Biologiskt Centrum, Umeå Universitet, SE 90187 Umeå, Sweden., Long Vo P; Institutionen för Kemi, Kemiskt Biologiskt Centrum, Umeå Universitet, SE 90187 Umeå, Sweden., Nilsson H; Institutionen för Kemi, Kemiskt Biologiskt Centrum, Umeå Universitet, SE 90187 Umeå, Sweden., Cheah MH; Institutionen för Kemi, Kemiskt Biologiskt Centrum, Umeå Universitet, SE 90187 Umeå, Sweden., Shevela D; Institutionen för Kemi, Kemiskt Biologiskt Centrum, Umeå Universitet, SE 90187 Umeå, Sweden., Saracini C; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Bean MA; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Seuffert I; Institut für Biologie, Humboldt-Universität zu Berlin, D-10099 Berlin, Germany., Sokaras D; SSRL, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Weng TC; SSRL, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Pastor E; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Weninger C; Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Fransson T; Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Lassalle L; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Bräuer P; Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.; Diamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK., Aller P; Diamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK., Docker PT; Diamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK., Andi B; National Synchrotron Light Source II, Brookhaven National Laboratory, Upton, NY, 11973, USA., Orville AM; Diamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK., Glownia JM; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Nelson S; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Sikorski M; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Zhu D; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Hunter MS; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Lane TJ; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Aquila A; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Koglin JE; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Robinson J; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Liang M; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Boutet S; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Lyubimov AY; Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA., Uervirojnangkoorn M; Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA., Moriarty NW; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Liebschner D; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Afonine PV; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Waterman DG; STFC Rutherford Appleton Laboratory, Didcot, OX11 0QX, UK and CCP4, Research Complex at Harwell, Rutherford Appleton Laboratory, Didcot, OX11 0FA, UK., Evans G; Diamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK., Wernet P; Institute for Methods and Instrumentation on Synchrotron Radiation Research, Helmholtz Zentrum, 14109 Berlin, Germany., Dobbek H; Institut für Biologie, Humboldt-Universität zu Berlin, D-10099 Berlin, Germany., Weis WI; Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA.; Department of Photon Science, Stanford University, Stanford, CA 94305.; Department of Structural Biology, Stanford University, Stanford, CA 94305., Brunger AT; Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA.; Department of Photon Science, Stanford University, Stanford, CA 94305., Zwart PH; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Adams PD; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.; Department of Bioengineering, University of California Berkeley, Berkeley, CA 94720., Zouni A; Institut für Biologie, Humboldt-Universität zu Berlin, D-10099 Berlin, Germany., Messinger J; Institutionen för Kemi, Kemiskt Biologiskt Centrum, Umeå Universitet, SE 90187 Umeå, Sweden.; Department of Chemistry, Molecular Biomimetics, Ångström Laboratory, Uppsala University, SE 75237 Uppsala, Sweden., Bergmann U; Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Sauter NK; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Kern J; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA., Yachandra VK; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Yano J; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Jazyk: angličtina
Zdroj: Nature [Nature] 2016 Dec 15; Vol. 540 (7633), pp. 453-457. Date of Electronic Publication: 2016 Nov 21.
DOI: 10.1038/nature20161
Abstrakt: Light-induced oxidation of water by photosystem II (PS II) in plants, algae and cyanobacteria has generated most of the dioxygen in the atmosphere. PS II, a membrane-bound multi-subunit pigment protein complex, couples the one-electron photochemistry at the reaction centre with the four-electron redox chemistry of water oxidation at the Mn 4 CaO 5 cluster in the oxygen-evolving complex (OEC). Under illumination, the OEC cycles through five intermediate S-states (S 0 to S 4 ), in which S 1 is the dark-stable state and S 3 is the last semi-stable state before O-O bond formation and O 2 evolution. A detailed understanding of the O-O bond formation mechanism remains a challenge, and will require elucidation of both the structures of the OEC in the different S-states and the binding of the two substrate waters to the catalytic site. Here we report the use of femtosecond pulses from an X-ray free electron laser (XFEL) to obtain damage-free, room temperature structures of dark-adapted (S 1 ), two-flash illuminated (2F; S 3 -enriched), and ammonia-bound two-flash illuminated (2F-NH 3 ; S 3 -enriched) PS II. Although the recent 1.95 Å resolution structure of PS II at cryogenic temperature using an XFEL provided a damage-free view of the S 1 state, measurements at room temperature are required to study the structural landscape of proteins under functional conditions, and also for in situ advancement of the S-states. To investigate the water-binding site(s), ammonia, a water analogue, has been used as a marker, as it binds to the Mn 4 CaO 5 cluster in the S 2 and S 3 states. Since the ammonia-bound OEC is active, the ammonia-binding Mn site is not a substrate water site. This approach, together with a comparison of the native dark and 2F states, is used to discriminate between proposed O-O bond formation mechanisms.
Databáze: MEDLINE
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