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.
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© 1992 Springer-Verlag Berlin Heidelberg
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Doig, S.J., Reid, P.J., Mathies, R.A. (1992). Picosecond Time-Resolved Resonance Raman Spectroscopy of Bacteriorhodopsin: Structure and Kinetics of the J, K, and KL Intermediates. In: Takahashi, H. (eds) Time-Resolved Vibrational Spectroscopy V. Springer Proceedings in Physics, vol 68. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-84771-4_14
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DOI: https://doi.org/10.1007/978-3-642-84771-4_14
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