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Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I.
Keable, Stephen M; Kölsch, Adrian; Simon, Philipp S; Dasgupta, Medhanjali; Chatterjee, Ruchira; Subramanian, Senthil Kumar; Hussein, Rana; Ibrahim, Mohamed; Kim, In-Sik; Bogacz, Isabel; Makita, Hiroki; Pham, Cindy C; Fuller, Franklin D; Gul, Sheraz; Paley, Daniel; Lassalle, Louise; Sutherlin, Kyle D; Bhowmick, Asmit; Moriarty, Nigel W; Young, Iris D; Blaschke, Johannes P; de Lichtenberg, Casper; Chernev, Petko; Cheah, Mun Hon; Park, Sehan; Park, Gisu; Kim, Jangwoo; Lee, Sang Jae; Park, Jaehyun; Tono, Kensuke; Owada, Shigeki; Hunter, Mark S; Batyuk, Alexander; Oggenfuss, Roland; Sander, Mathias; Zerdane, Serhane; Ozerov, Dmitry; Nass, Karol; Lemke, Henrik; Mankowsky, Roman; Brewster, Aaron S; Messinger, Johannes; Sauter, Nicholas K; Yachandra, Vittal K; Yano, Junko; Zouni, Athina; Kern, Jan.
Afiliación
  • Keable SM; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Kölsch A; Institut für Biologie, Humboldt-Universität Zu Berlin, 10115, Berlin, Germany.
  • Simon PS; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Dasgupta M; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Chatterjee R; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Subramanian SK; Institut für Biologie, Humboldt-Universität Zu Berlin, 10115, Berlin, Germany.
  • Hussein R; Institut für Biologie, Humboldt-Universität Zu Berlin, 10115, Berlin, Germany.
  • Ibrahim M; Institut für Biologie, Humboldt-Universität Zu Berlin, 10115, Berlin, Germany.
  • Kim IS; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Bogacz I; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Makita H; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Pham CC; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Fuller FD; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA, 94025, USA.
  • Gul S; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Paley D; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Lassalle L; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Sutherlin KD; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Bhowmick A; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Moriarty NW; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Young ID; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Blaschke JP; Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA, 94158, USA.
  • de Lichtenberg C; National Energy Research Scientific Computing Center, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Chernev P; Department of Chemistry - Ångström, Molecular Biomimetics, Uppsala University, 75237, Uppsala, Sweden.
  • Cheah MH; Department of Chemistry, Umeå University, Linnaeus väg 6 (KBC huset), 90187, Umeå, Sweden.
  • Park S; Department of Chemistry - Ångström, Molecular Biomimetics, Uppsala University, 75237, Uppsala, Sweden.
  • Park G; Department of Chemistry - Ångström, Molecular Biomimetics, Uppsala University, 75237, Uppsala, Sweden.
  • Kim J; Pohang Accelerator Laboratory, POSTECH, Pohang, 37673, Korea.
  • Lee SJ; Pohang Accelerator Laboratory, POSTECH, Pohang, 37673, Korea.
  • Park J; Pohang Accelerator Laboratory, POSTECH, Pohang, 37673, Korea.
  • Tono K; Pohang Accelerator Laboratory, POSTECH, Pohang, 37673, Korea.
  • Owada S; Pohang Accelerator Laboratory, POSTECH, Pohang, 37673, Korea.
  • Hunter MS; Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo, 679-5198, Japan.
  • Batyuk A; RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo, 679-5148, Japan.
  • Oggenfuss R; Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo, 679-5198, Japan.
  • Sander M; RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo, 679-5148, Japan.
  • Zerdane S; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA, 94025, USA.
  • Ozerov D; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA, 94025, USA.
  • Nass K; Paul Scherrer Institut, 5232, Villigen, Switzerland.
  • Lemke H; Paul Scherrer Institut, 5232, Villigen, Switzerland.
  • Mankowsky R; Paul Scherrer Institut, 5232, Villigen, Switzerland.
  • Brewster AS; Paul Scherrer Institut, 5232, Villigen, Switzerland.
  • Messinger J; Paul Scherrer Institut, 5232, Villigen, Switzerland.
  • Sauter NK; Paul Scherrer Institut, 5232, Villigen, Switzerland.
  • Yachandra VK; Paul Scherrer Institut, 5232, Villigen, Switzerland.
  • Yano J; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
  • Zouni A; Department of Chemistry - Ångström, Molecular Biomimetics, Uppsala University, 75237, Uppsala, Sweden.
  • Kern J; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.
Sci Rep ; 11(1): 21787, 2021 11 08.
Article en En | MEDLINE | ID: mdl-34750381
ABSTRACT
Photosystem I (PS I) has a symmetric structure with two highly similar branches of pigments at the center that are involved in electron transfer, but shows very different efficiency along the two branches. We have determined the structure of cyanobacterial PS I at room temperature (RT) using femtosecond X-ray pulses from an X-ray free electron laser (XFEL) that shows a clear expansion of the entire protein complex in the direction of the membrane plane, when compared to previous cryogenic structures. This trend was observed by complementary datasets taken at multiple XFEL beamlines. In the RT structure of PS I, we also observe conformational differences between the two branches in the reaction center around the secondary electron acceptors A1A and A1B. The π-stacked Phe residues are rotated with a more parallel orientation in the A-branch and an almost perpendicular confirmation in the B-branch, and the symmetry breaking PsaB-Trp673 is tilted and further away from A1A. These changes increase the asymmetry between the branches and may provide insights into the preferential directionality of electron transfer.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Vitamina K 1 / Complejo de Proteína del Fotosistema I Idioma: En Revista: Sci Rep Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Vitamina K 1 / Complejo de Proteína del Fotosistema I Idioma: En Revista: Sci Rep Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos