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Biophysical Journal 53: 465-468 (1988)
© 1988 the Biophysical Society

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A time-resolved spectral study of the K and KL intermediates of bacteriorhodopsin.

S J Milder and D S Kliger

Department of Chemistry, University of California, Santa Cruz 95064.

ABSTRACT

Nanosecond time-resolved absorption measurements on the photolysis products of bacteriorhodopsin (BR) in intact membranes are reported. At room temperature in fluid solution a single intermediate (KL) is seen 10 ns after excitation. Both spectral and kinetic results are consistent with the KL intermediate converting to the L intermediate by a single first order reaction. The observed temperature-dependent rate has the Arrhenius parameters: Ea = 10.5 kcal/mol, A = 5 x 10(13) s-1. The precursor to the KL intermediate is also observed. Its spectral character is consistent with the K intermediate which has been previously reported. The current data is consistent with a linear sequence in the BR photocycle for K, KL, and L in room temperature fluid solution. Differences in the spectral characteristics of the K intermediates described here and elsewhere are discussed in terms of differences in the microenvironment around the retinal moiety and the affect this may have on the conformation of the chromophore.




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J. Xu, A. B. Stickrath, P. Bhattacharya, J. Nees, G. Varo, J. R. Hillebrecht, L. Ren, and R. R. Birge
Direct Measurement of the Photoelectric Response Time of Bacteriorhodopsin via Electro-Optic Sampling
Biophys. J., August 1, 2003; 85(2): 1128 - 1134.
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Copyright © 1988 by the Biophysical Society.