Special Articles

Chemical Dynamics in Proteins: The Photoisomerization of Retinal in Bacteriorhodopsin

See allHide authors and affiliations

Science  20 Mar 1998:
Vol. 279, Issue 5358, pp. 1886-1891
DOI: 10.1126/science.279.5358.1886

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

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.

  • * Present address: Los Alamos National Laboratory, CST-4, MS J586, Los Alamos, NM 87545, USA.

  • Present address: Magnetic Imaging Technologies, 2500 Meridian Parkway, Suite 175, Durham, NC 27713, USA.

  • To whom correspondence should be addressed. E-mail: anfinrud{at}chemistry.harvard.edu

View Full Text