Chemical Dynamics in Proteins: The Photoisomerization of Retinal in Bacteriorhodopsin

Author:

Gai Feng1,Hasson K. C.1,McDonald J. Cooper1,Anfinrud Philip A.1

Affiliation:

1. The authors are in the Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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