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Ultrafast Protein Dynamics of Bacteriorhodopsin Probed by Photon Echo and Transient Absorption Spectroscopy
| Content Provider | Semantic Scholar |
|---|---|
| Author | Kennis, John T. M. Larsen, Delmar S. Ohta, Kaoru Facciotti, Marc T. Glaeser, Robert M. Fleming, Graham R. |
| Copyright Year | 2002 |
| Abstract | Bacteriorhodopsin (bR) is an efficient light-driven proton pump which shows a trans-cis isomerization reaction of its retinal chromophore after light absorption. BR exhibits a large reorganization energy λ of 2520 cm-1 on optical excitation. In this paper, we have studied the nature, origin, and dynamical aspects of this extensive reorganization. We report the results of a femtosecond three-pulse echo peak shift (3PEPS), transient grating (TG) and transient absorption (TA) study, complemented with those of steady-state absorption and fluorescence spectroscopy in wild-type bR and the D85S mutant in its blue and purple, halide-pumping forms. We have simulated the results in the context of the multimode Brownian oscillator (MBO) formalism. A simple model that incorporates retinal's known intramolecular vibrations, which represent 1094 cm-1 or reorganization energy, and a single Gaussian protein relaxation with a decay of 50 fs representing 1430 cm-1 of reorganization energy, yielded satisfactory results for ... |
| Starting Page | 6067 |
| Ending Page | 6080 |
| Page Count | 14 |
| File Format | PDF HTM / HTML |
| DOI | 10.1021/jp014681b |
| Alternate Webpage(s) | http://www.cchem.berkeley.edu/grfgrp/Papers/2002%20Kennis%20JPhysChemB106.pdf |
| Alternate Webpage(s) | https://doi.org/10.1021/jp014681b |
| Volume Number | 106 |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
