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Structural evidence for intermediates during O2 formation in photosystem II.
Bhowmick, Asmit; Hussein, Rana; Bogacz, Isabel; Simon, Philipp S; Ibrahim, Mohamed; Chatterjee, Ruchira; Doyle, Margaret D; Cheah, Mun Hon; Fransson, Thomas; Chernev, Petko; Kim, In-Sik; Makita, Hiroki; Dasgupta, Medhanjali; Kaminsky, Corey J; Zhang, Miao; Gätcke, Julia; Haupt, Stephanie; Nangca, Isabela I; Keable, Stephen M; Aydin, A Orkun; Tono, Kensuke; Owada, Shigeki; Gee, Leland B; Fuller, Franklin D; Batyuk, Alexander; Alonso-Mori, Roberto; Holton, James M; Paley, Daniel W; Moriarty, Nigel W; Mamedov, Fikret; Adams, Paul D; Brewster, Aaron S; Dobbek, Holger; Sauter, Nicholas K; Bergmann, Uwe; Zouni, Athina; Messinger, Johannes; Kern, Jan; Yano, Junko; Yachandra, Vittal K.
Afiliação
  • Bhowmick A; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Hussein R; Department of Biology, Humboldt Universität zu Berlin, Berlin, Germany.
  • Bogacz I; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Simon PS; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Ibrahim M; Department of Biology, Humboldt Universität zu Berlin, Berlin, Germany.
  • Chatterjee R; Institute of Molecular Medicine, University of Lübeck, Lübeck, Germany.
  • Doyle MD; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Cheah MH; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Fransson T; Molecular Biomimetics, Department of Chemistry - Ångström, Uppsala University, Uppsala, Sweden.
  • Chernev P; Department of Theoretical Chemistry and Biology, KTH Royal Institute of Technology, Stockholm, Sweden.
  • Kim IS; Molecular Biomimetics, Department of Chemistry - Ångström, Uppsala University, Uppsala, Sweden.
  • Makita H; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Dasgupta M; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Kaminsky CJ; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Zhang M; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Gätcke J; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Haupt S; Department of Biology, Humboldt Universität zu Berlin, Berlin, Germany.
  • Nangca II; Department of Biology, Humboldt Universität zu Berlin, Berlin, Germany.
  • Keable SM; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Aydin AO; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Tono K; Molecular Biomimetics, Department of Chemistry - Ångström, Uppsala University, Uppsala, Sweden.
  • Owada S; Japan Synchrotron Radiation Research Institute, Hyogo, Japan.
  • Gee LB; RIKEN SPring-8 Center, Hyogo, Japan.
  • Fuller FD; Japan Synchrotron Radiation Research Institute, Hyogo, Japan.
  • Batyuk A; RIKEN SPring-8 Center, Hyogo, Japan.
  • Alonso-Mori R; Linac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
  • Holton JM; Linac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
  • Paley DW; Linac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
  • Moriarty NW; Linac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
  • Mamedov F; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Adams PD; Department of Biochemistry and Biophysics, University of California, San Francisco, CA, USA.
  • Brewster AS; SSRL, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
  • Dobbek H; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Sauter NK; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Bergmann U; Molecular Biomimetics, Department of Chemistry - Ångström, Uppsala University, Uppsala, Sweden.
  • Zouni A; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Messinger J; Department of Bioengineering, University of California, Berkeley, CA, USA.
  • Kern J; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
  • Yano J; Department of Biology, Humboldt Universität zu Berlin, Berlin, Germany.
  • Yachandra VK; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
Nature ; 617(7961): 629-636, 2023 May.
Article em En | MEDLINE | ID: mdl-37138085
ABSTRACT
In natural photosynthesis, the light-driven splitting of water into electrons, protons and molecular oxygen forms the first step of the solar-to-chemical energy conversion process. The reaction takes place in photosystem II, where the Mn4CaO5 cluster first stores four oxidizing equivalents, the S0 to S4 intermediate states in the Kok cycle, sequentially generated by photochemical charge separations in the reaction center and then catalyzes the O-O bond formation chemistry1-3. Here, we report room temperature snapshots by serial femtosecond X-ray crystallography to provide structural insights into the final reaction step of Kok's photosynthetic water oxidation cycle, the S3→[S4]→S0 transition where O2 is formed and Kok's water oxidation clock is reset. Our data reveal a complex sequence of events, which occur over micro- to milliseconds, comprising changes at the Mn4CaO5 cluster, its ligands and water pathways as well as controlled proton release through the hydrogen-bonding network of the Cl1 channel. Importantly, the extra O atom Ox, which was introduced as a bridging ligand between Ca and Mn1 during the S2→S3 transition4-6, disappears or relocates in parallel with Yz reduction starting at approximately 700 µs after the third flash. The onset of O2 evolution, as indicated by the shortening of the Mn1-Mn4 distance, occurs at around 1,200 µs, signifying the presence of a reduced intermediate, possibly a bound peroxide.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Oxigênio / Fotossíntese / Complexo de Proteína do Fotossistema II Idioma: En Revista: Nature Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Estados Unidos
Texto completo
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PubMed Links
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Oxigênio / Fotossíntese / Complexo de Proteína do Fotossistema II Idioma: En Revista: Nature Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Estados Unidos