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SUMMARY:Keynote 3\, Prof. Richard Neutze: Time-resolved diffraction experi
 ments at X-ray free electron lasers reveal ultrafast structural changes in
  photosynthesis
DTSTART;VALUE=DATE-TIME:20191009T144500Z
DTEND;VALUE=DATE-TIME:20191009T152500Z
DTSTAMP;VALUE=DATE-TIME:20260525T195342Z
UID:indico-contribution-758@lindico453.srv.lu.se
DESCRIPTION:Speakers: Richard Neutze (Gothenburg University)\nX-ray free e
 lectron lasers (XFEL) have sparked the development of time-resolved serial
  femtosecond crystallography (TR-SFX)\, which is a completely new experime
 ntal approach to understanding protein structural dynamics. We have used T
 R-SFX at the LCLS (an XFEL in California) to probe light-driven structural
  changes from picoseconds to microseconds in a bacterial photosynthetic re
 action centre. These integral membrane proteins harvest sunlight in order 
 to transfer electrons from a special pair of bacteriochlorophylls to quino
 ne molecules that are located on the opposite side of an energy transducin
 g biological membrane. Coupled redox reactions balance the charges and thi
 s leads to a net effect of two pumped protons per photon absorbed. TR-SFX 
 studies at the LCLS revealed structural changes on the picosecond time-sca
 le near the special pair (which is photo-oxidized by light) and the tightl
 y bound menaquinone (which accepts an electron from the special pair). The
 se structural results provide novel chemical insight into how protein stru
 ctural dynamics are able to help to stabilize the charge separated state. 
 With the extension of serial crystallography to synchrotron radiation sour
 ces\, I argue that time-resolved diffraction studies will become more comm
 on in the future as new approaches allow new biological systems to be prob
 ed.\n\nhttps://lindico453.srv.lu.se/event/125/contributions/758/
LOCATION:Kulturen Auditorium
URL:https://lindico453.srv.lu.se/event/125/contributions/758/
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