Scientific Reports (Nov 2021)
Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I
- Stephen M. Keable,
- Adrian Kölsch,
- Philipp S. Simon,
- Medhanjali Dasgupta,
- Ruchira Chatterjee,
- Senthil Kumar Subramanian,
- Rana Hussein,
- Mohamed Ibrahim,
- In-Sik Kim,
- Isabel Bogacz,
- Hiroki Makita,
- Cindy C. Pham,
- Franklin D. Fuller,
- Sheraz Gul,
- Daniel Paley,
- Louise Lassalle,
- Kyle D. Sutherlin,
- Asmit Bhowmick,
- Nigel W. Moriarty,
- Iris D. Young,
- Johannes P. Blaschke,
- Casper de Lichtenberg,
- Petko Chernev,
- Mun Hon Cheah,
- Sehan Park,
- Gisu Park,
- Jangwoo Kim,
- Sang Jae Lee,
- Jaehyun Park,
- Kensuke Tono,
- Shigeki Owada,
- Mark S. Hunter,
- Alexander Batyuk,
- Roland Oggenfuss,
- Mathias Sander,
- Serhane Zerdane,
- Dmitry Ozerov,
- Karol Nass,
- Henrik Lemke,
- Roman Mankowsky,
- Aaron S. Brewster,
- Johannes Messinger,
- Nicholas K. Sauter,
- Vittal K. Yachandra,
- Junko Yano,
- Athina Zouni,
- Jan Kern
Affiliations
- Stephen M. Keable
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Adrian Kölsch
- Institut für Biologie, Humboldt-Universität Zu Berlin
- Philipp S. Simon
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Medhanjali Dasgupta
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Ruchira Chatterjee
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Senthil Kumar Subramanian
- Institut für Biologie, Humboldt-Universität Zu Berlin
- Rana Hussein
- Institut für Biologie, Humboldt-Universität Zu Berlin
- Mohamed Ibrahim
- Institut für Biologie, Humboldt-Universität Zu Berlin
- In-Sik Kim
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Isabel Bogacz
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Hiroki Makita
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Cindy C. Pham
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Franklin D. Fuller
- LCLS, SLAC National Accelerator Laboratory
- Sheraz Gul
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Daniel Paley
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Louise Lassalle
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Kyle D. Sutherlin
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Asmit Bhowmick
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Nigel W. Moriarty
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Iris D. Young
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Johannes P. Blaschke
- National Energy Research Scientific Computing Center, Lawrence Berkeley National Laboratory
- Casper de Lichtenberg
- Department of Chemistry - Ångström, Molecular Biomimetics, Uppsala University
- Petko Chernev
- Department of Chemistry - Ångström, Molecular Biomimetics, Uppsala University
- Mun Hon Cheah
- Department of Chemistry - Ångström, Molecular Biomimetics, Uppsala University
- Sehan Park
- Pohang Accelerator Laboratory, POSTECH
- Gisu Park
- Pohang Accelerator Laboratory, POSTECH
- Jangwoo Kim
- Pohang Accelerator Laboratory, POSTECH
- Sang Jae Lee
- Pohang Accelerator Laboratory, POSTECH
- Jaehyun Park
- Pohang Accelerator Laboratory, POSTECH
- Kensuke Tono
- Japan Synchrotron Radiation Research Institute
- Shigeki Owada
- Japan Synchrotron Radiation Research Institute
- Mark S. Hunter
- LCLS, SLAC National Accelerator Laboratory
- Alexander Batyuk
- LCLS, SLAC National Accelerator Laboratory
- Roland Oggenfuss
- Paul Scherrer Institut
- Mathias Sander
- Paul Scherrer Institut
- Serhane Zerdane
- Paul Scherrer Institut
- Dmitry Ozerov
- Paul Scherrer Institut
- Karol Nass
- Paul Scherrer Institut
- Henrik Lemke
- Paul Scherrer Institut
- Roman Mankowsky
- Paul Scherrer Institut
- Aaron S. Brewster
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Johannes Messinger
- Department of Chemistry - Ångström, Molecular Biomimetics, Uppsala University
- Nicholas K. Sauter
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Vittal K. Yachandra
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Junko Yano
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- Athina Zouni
- Institut für Biologie, Humboldt-Universität Zu Berlin
- Jan Kern
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory
- DOI
- https://doi.org/10.1038/s41598-021-00236-3
- Journal volume & issue
-
Vol. 11,
no. 1
pp. 1 – 14
Abstract
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.
