1 December 2001 Spectroscopic Characterization of Bacteriorhodopsin's L-intermediate in 3D Crystals Cooled to 170 K
Antoine Royant, Karl Edman, Thomas Ursby, Eva Pebay-Peyroula, EhudM. Landau, Richard Neutze
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Abstract

Spectra are presented from a single 3D microcrystal of bacteriorhodopsin (bR) cooled to 170 K under various illumination conditions. This set is necessary and sufficient to assign the relevant crystal reference spectra. A spectral decomposition of the difference spectrum obtained following the trapping protocol of Royant et al. (2000) (Nature 406, 645–648) is given, confirming that the low temperature L-intermediate was the species that dominated the structural rearrangements previously reported. Smaller contributions from the K and M spectral intermediates are also quantified. Mechanistic insights derived from the X-ray structures of the early bR intermediates are discussed.

Antoine Royant, Karl Edman, Thomas Ursby, Eva Pebay-Peyroula, EhudM. Landau, and Richard Neutze "Spectroscopic Characterization of Bacteriorhodopsin's L-intermediate in 3D Crystals Cooled to 170 K," Photochemistry and Photobiology 74(6), 794-804, (1 December 2001). https://doi.org/10.1562/0031-8655(2001)074<0794:SCOBSL>2.0.CO;2
Received: 2 May 2001; Accepted: 1 September 2001; Published: 1 December 2001
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