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Chemical Dynamics in Proteins: The Photoisomerization of Retinal in Bacteriorhodopsin

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

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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

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