| Literature DB >> 33268896 |
Robert Dods1, Petra Båth1, Dmitry Morozov2, Viktor Ahlberg Gagnér1, David Arnlund1, Hoi Ling Luk2, Joachim Kübel1, Michał Maj1, Adams Vallejos1, Cecilia Wickstrand1, Robert Bosman1, Kenneth R Beyerlein3, Garrett Nelson4, Mengning Liang5, Despina Milathianaki5, Joseph Robinson5, Rajiv Harimoorthy1, Peter Berntsen1,6, Erik Malmerberg7, Linda Johansson1,8, Rebecka Andersson1, Sergio Carbajo5, Elin Claesson1, Chelsie E Conrad9, Peter Dahl1, Greger Hammarin1, Mark S Hunter5, Chufeng Li4, Stella Lisova4, Antoine Royant10,11, Cecilia Safari1, Amit Sharma1, Garth J Williams5, Oleksandr Yefanov3, Sebastian Westenhoff1, Jan Davidsson12, Daniel P DePonte5, Sébastien Boutet5, Anton Barty3, Gergely Katona1, Gerrit Groenhof2, Gisela Brändén1, Richard Neutze13.
Abstract
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.Entities:
Year: 2020 PMID： 33268896 DOI： 10.1038/s41586-020-3000-7
Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962