4.8 Article

Ultrafast structural changes within a photosynthetic reaction centre

期刊

NATURE
卷 589, 期 7841, 页码 310-+

出版社

NATURE PORTFOLIO
DOI: 10.1038/s41586-020-3000-7

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资金

  1. US Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
  2. NIH [P41GM103393]
  3. European Commission Marie Curie Training Networks (X-Probe, NanoMem)
  4. European Union's Horizon 2020 research and innovation programme [789030]
  5. Swedish Research Council [2015-00560, 349-2011-6485, 2017-06734]
  6. Swedish Foundation for Strategic Research [SRL10-0036, ID17-0060]
  7. Knut and Alice Wallenberg Foundation [KAW 2012.0284, KAW 2012.0275, KAW 2014.0275]
  8. Academy of Finland [290677, 304455]
  9. BioExcel CoE project - European Union [H2020-INFRAEDI-02-2018-823830, H2020-EINFRA-2015-1-675728]
  10. Swedish Research Council [2017-06734] Funding Source: Swedish Research Council
  11. Swedish Foundation for Strategic Research (SSF) [ID17-0060, SRL10-0036] Funding Source: Swedish Foundation for Strategic Research (SSF)
  12. Academy of Finland (AKA) [304455, 304455] Funding Source: Academy of Finland (AKA)
  13. European Research Council (ERC) [789030] Funding Source: European Research Council (ERC)

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Time-resolved serial femtosecond crystallography is used to observe light-induced structural changes in the photosynthetic reaction center of Blastochloris viridis on a picosecond timescale, revealing how proteins stabilize charge-separation steps of electron-transfer reactions through conformational dynamics.
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 crystallography(1) using an X-ray free-electron laser(2) 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. Time-resolved serial femtosecond crystallography is used to reveal the structural changes that stabilize the charge-separation steps of electron-transfer reactions in the photosynthetic reaction centre of Blastochloris viridis on a timescale of picoseconds.

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