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Resonance Raman Structural Evidence that the Cis-to-Trans Isomerization in Rhodopsin Occurs in Femtoseconds.

J E Kim1, D W McCamant, L Zhu

  • 1Department of Chemistry, University of California, Berkeley, California 94720.

The Journal of Physical Chemistry. B
|June 7, 2006
PubMed
Summary
This summary is machine-generated.

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Vision begins with rhodopsin

Area of Science:

  • Biophysics
  • Photochemistry
  • Spectroscopy

Background:

  • Vision initiates with the cis-to-trans isomerization of rhodopsin's retinal chromophore.
  • Understanding the ultrafast structural dynamics of this process is crucial for deciphering the initial steps of vision.

Purpose of the Study:

  • To investigate the structural changes of rhodopsin's retinal chromophore during cis-to-trans isomerization.
  • To elucidate the temporal evolution of the chromophore's configuration in the picosecond timescale.

Main Methods:

  • Picosecond time-resolved resonance Raman spectroscopy was employed.
  • Pump-probe experiments utilized 2.2 ps, 480 nm pump and 1.5 ps, 600 nm probe pulses.
  • Spectra were recorded at various time delays from -0.7 to 20.8 ps.

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Main Results:

  • Evidence of a strained, all-trans chromophore (photorhodopsin) within 0.8 ps of photon absorption.
  • Kinetic analysis revealed fast (~200 fs) and slow (~2-3 ps) components in spectral feature growth.
  • Chromophore cooling and relaxation to bathorhodopsin occurred within picoseconds, indicated by spectral shifts and narrowing.

Conclusions:

  • The study provides the first structural evidence for a thermally unrelaxed, torsionally strained all-trans chromophore forming within picoseconds.
  • Ultrafast photorhodopsin formation is coupled with a rapid, localized protein response.
  • The protein complex stores significant photon energy, driving subsequent activating conformational changes.