Ultrafast structural changes within a photosynthetic reaction centre
Dods, R., Båth, P., Morozov, D., Gagnér, V. A., Arnlund, D., Luk, H. L., Kübel, J., Maj, M., Vallejos, A., Wickstrand, C., Bosman, R., Beyerlein, K. R., Nelson, G., Liang, M., Milathianaki, D., Robinson, J., Harimoorthy, R., Berntsen, P., Malmerberg, E., . . . Neutze, R. (2021). Ultrafast structural changes within a photosynthetic reaction centre. Nature, 589(7841), 310-314. https://doi.org/10.1038/s41586-020-3000-7
© Nature Publishing Group, 2020
Photosynthetic reaction centres harvest the energy content of sunlight by transporting electrons across an energy-transducing biological membrane. Here we use time-resolved serial femtosecond crystallography1 using an X-ray free-electron laser2 to observe light-induced structural changes in the photosynthetic reaction centre of Blastochloris viridis on a timescale of picoseconds. Structural perturbations first occur at the special pair of chlorophyll molecules of the photosynthetic reaction centre that are photo-oxidized by light. Electron transfer to the menaquinone acceptor on the opposite side of the membrane induces a movement of this cofactor together with lower amplitude protein rearrangements. These observations reveal how proteins use conformational dynamics to stabilize the charge-separation steps of electron-transfer reactions.
PublisherNature Publishing Group
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Related funder(s)Academy of Finland
Funding program(s)Others, AoF; Academy Project, AoF
Additional information about fundingUse of the Linac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory, is supported by the US Department of Energy, Office of Science, Office of Basic Energy Sciences under contract no. DE-AC02-76SF00515. Parts of the sample delivery system used at LCLS for this research were funded by NIH grant P41GM103393, formerly P41RR001209. Complementary studies were performed at BL3 of SACLA with the approval of the Japan Synchrotron Radiation Research Institute (JASRI, proposal number 2018B8068). R.N. acknowledges funding from the European Commission Marie Curie Training Networks (X-Probe, NanoMem), the European Union’s Horizon 2020 research and innovation programme (grant agreement 789030) and the Swedish Research Council (grants 2015-00560 and 349-2011-6485), the Swedish Foundation for Strategic Research (grant SRL10-0036), and the Knut and Alice Wallenberg Foundation (grant KAW 2012.0284, KAW 2012.0275 and KAW 2014.0275). G.B. acknowledges funding from the Swedish Research Council (grant 2017-06734) and the Swedish Foundation for Strategic Research (grant ID17-0060). G.G., D. Morozov and H.L.L. acknowledge funding from the Academy of Finland (grants 290677 and 304455), the BioExcel CoE project funded by the European Union contracts H2020-INFRAEDI-02-2018-823830 and H2020-EINFRA-2015-1-675728, and the CSC-IT centre in Espoo for access to computing resources. R.N. thanks N. Woodbury for discussions. ...
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