Bathorhodopsin structure in the room-temperature rhodopsin photosequence: picosecond time-resolved coherent anti-Stokes Raman scattering

Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):372-6. doi: 10.1073/pnas.93.1.372.

Abstract

Structural changes in the retinal chromophore during the formation of the bathorhodopsin intermediate (bathoRT) in the room-temperature rhodopsin (RhRT) photosequence (i.e., vision) are examined using picosecond time-resolved coherent anti-Stokes Raman scattering. Specifically, the retinal structure assignable to bathoRT following 8-ps excitation of RhRT is measured via vibrational Raman spectroscopy at a 200-ps time delay where the only intermediate present is bathoRT. Significant differences are observed between the C=C stretching frequencies of the retinal chromophore at low temperature where bathorhodopsin is stabilized and at room temperature where bathorhodopsin is a transient species in the RhRT photosequence. These vibrational data are discussed in terms of the formation of bathoRT, an important step in the energy storage/transduction mechanism of RhRT.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cattle
  • Chemical Phenomena
  • Chemistry, Physical
  • Motion
  • Photochemistry
  • Rhodopsin / analogs & derivatives*
  • Rhodopsin / chemistry*
  • Scattering, Radiation
  • Spectrum Analysis, Raman / methods
  • Temperature

Substances

  • bathorhodopsin
  • Rhodopsin