期刊
NATURE
卷 589, 期 7841, 页码 310-+出版社
NATURE PORTFOLIO
DOI: 10.1038/s41586-020-3000-7
关键词
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资金
- US Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- NIH [P41GM103393]
- European Commission Marie Curie Training Networks (X-Probe, NanoMem)
- European Union's Horizon 2020 research and innovation programme [789030]
- Swedish Research Council [2015-00560, 349-2011-6485, 2017-06734]
- Swedish Foundation for Strategic Research [SRL10-0036, ID17-0060]
- Knut and Alice Wallenberg Foundation [KAW 2012.0284, KAW 2012.0275, KAW 2014.0275]
- Academy of Finland [290677, 304455]
- BioExcel CoE project - European Union [H2020-INFRAEDI-02-2018-823830, H2020-EINFRA-2015-1-675728]
- Swedish Research Council [2017-06734] Funding Source: Swedish Research Council
- Swedish Foundation for Strategic Research (SSF) [ID17-0060, SRL10-0036] Funding Source: Swedish Foundation for Strategic Research (SSF)
- Academy of Finland (AKA) [304455, 304455] Funding Source: Academy of Finland (AKA)
- European Research Council (ERC) [789030] Funding Source: European Research Council (ERC)
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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