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Ultrafast Protein Dynamics Prior to Retinal Photoisomerization in Microbial Rhodopsins.

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Ultrafast protein structural changes precede chromophore photoisomerization in rhodopsins. This finding, observed in H+-pump rhodopsin and photosensor rhodopsin, suggests a conserved mechanism across different rhodopsin types.

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Area of Science:

  • Biochemistry
  • Spectroscopy
  • Structural Biology

Background:

  • Rhodopsins are photoreceptor proteins crucial for vision and energy transduction.
  • The photoisomerization of the retinal chromophore was traditionally considered the primary photoactivation event.
  • Recent studies suggested protein structural changes may precede chromophore isomerization in bacteriorhodopsin.

Purpose of the Study:

  • To investigate if ultrafast protein structural changes preceding chromophore photoisomerization are common in rhodopsins.
  • To examine these dynamics in H+-pump rhodopsin (RxR) and photosensor rhodopsin (NpSRII).

Main Methods:

  • Deep-ultraviolet femtosecond stimulated Raman spectroscopy was employed.
  • Ultrafast spectroscopic measurements were performed on RxR and NpSRII.

Main Results:

  • Protein structural changes were observed to occur within 0.2 picoseconds after photoexcitation.
  • These protein dynamics consistently preceded chromophore photoisomerization in both RxR and NpSRII.
  • Limited protein structural changes occurred on the timescale of photoisomerization, indicating a pre-optimized protein environment.

Conclusions:

  • Ultrafast protein structural changes precede chromophore photoisomerization in rhodopsins, irrespective of their function or origin.
  • This suggests a conserved mechanism in rhodopsin photocycles.
  • The protein environment may be pre-arranged by these early structural changes to facilitate subsequent chromophore isomerization.