Chemical dynamics in proteins: The photoisomerization of retinal in bacteriorhodopsin

被引:229
作者
Gai, F [1 ]
Hasson, KC [1 ]
McDonald, JC [1 ]
Anfinrud, PA [1 ]
机构
[1] Harvard Univ, Dept Chem & Biol Chem, Cambridge, MA 02138 USA
关键词
D O I
10.1126/science.279.5358.1886
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:1886 / 1891
页数:6
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