Chemical dynamics in proteins: the photoisomerization of retinal in bacteriorhodopsin

Science. 1998 Mar 20;279(5358):1886-91. doi: 10.1126/science.279.5358.1886.

Abstract

Chemical dynamics in proteins are discussed, with bacteriorhodopsin serving as a model system. Ultrafast time-resolved methods used to probe the chemical dynamics of retinal photoisomerization in bacteriorhodopsin are discussed, along with future prospects for ultrafast time-resolved crystallography. The photoisomerization of retinal in bacteriorhodopsin is far more selective and efficient than in solution, the origins of which are discussed in the context of a three-state model for the photoisomerization reaction coordinate. The chemical dynamics are complex, with the excited-state relaxation exhibiting a multiexponential decay with well-defined rate constants. Possible origins for the two major components are also discussed.

Publication types

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

MeSH terms

  • Bacteriorhodopsins / chemistry*
  • Bacteriorhodopsins / metabolism
  • Diterpenes
  • Halobacterium salinarum / chemistry
  • Halobacterium salinarum / metabolism
  • Isomerism
  • Kinetics
  • Light*
  • Models, Chemical
  • Protein Conformation
  • Retinaldehyde / chemistry*
  • Retinaldehyde / metabolism
  • Spectrum Analysis
  • Thermodynamics

Substances

  • Diterpenes
  • 13-cis-retinal
  • Bacteriorhodopsins
  • Retinaldehyde