Picosecond Time-Resolved Resonance Raman Spectroscopy of Bacteriorhodopsin: Structure and Kinetics of the J, K, and KL Intermediates

  • S. J. Doig
  • P. J. Reid
  • R. A. Mathies
Part of the Springer Proceedings in Physics book series (SPPHY, volume 68)

Abstract

Bacteriorhodopsin (BR) is an intrinsic membrane protein that functions as a light-driven proton pump [1]. Light absorption by its all-trans retinal protonated Schiff base prosthetic group initiates a trans → 13-cis isomerization. The first ground-state photoproduct, called J, forms in only 500 fs [2]. J decays to the K intermediate in 3 ps [3] which forms L in about 1 μs. The structural changes of the chromophore that accompany the J to K transition are not well defined. Also, although some studies have suggested the presence of an additional intermediate between K and L called “KL” [4, 5], this transition has not been characterized.

Keywords

Argon Autocorrelation Convolution Photolysis Schiff 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1992

Authors and Affiliations

  • S. J. Doig
    • 1
  • P. J. Reid
    • 1
  • R. A. Mathies
    • 1
  1. 1.Chemistry DepartmentUniversity of CaliforniaBerkeleyUSA

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