Bacteriorhodopsin: Structural insights revealed using x-ray lasers and synchrotron radiation

Cecilia Wickstrand, Przemyslaw Nogly, Eriko Nango, So Iwata, Jörg Standfuss, Richard Neutze

Research output: Contribution to journalReview articlepeer-review

37 Citations (Scopus)


Directional transport of protons across an energy transducing membrane-proton pumping-is ubiquitous in biology. Bacteriorhodopsin (bR) is a light-driven proton pump that is activated by a buried all-trans retinal chromophore being photoisomerized to a 13-cis conformation. The mechanism by which photoisomerization initiates directional proton transport against a proton concentration gradient has been studied by a myriad of biochemical, biophysical, and structural techniques. X-ray free electron lasers (XFELs) have created new opportunities to probe the structural dynamics of bR at room temperature on timescales from femtoseconds to milliseconds using time-resolved serial femtosecond crystallography (TR-SFX). Wereview these recent developments and highlight where XFEL studies reveal new details concerning the structural mechanism of retinal photoisomerization and proton pumping. We also discuss the extent to which these insights were anticipated by earlier intermediate trapping studies using synchrotron radiation. TR-SFX will open up the field for dynamical studies of other proteins that are not naturally light-sensitive.

Original languageEnglish
Pages (from-to)59-83
Number of pages25
JournalAnnual Review of Biochemistry
Publication statusPublished - 2019 Jun 20


  • bacteriorhodopsin
  • bioenergetics
  • intermediate trapping
  • proton pumping
  • time-resolved serial femtosecond crystallography
  • X-ray free electron lasers


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