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Proceedings Paper

Picosecond time-resolved resonance Raman spectroscopy of bacteriorhodopsin: structure and kinetics of the J, K, and KL intermediates
Author(s): Stephen J. Doig; Philip J. Reid; Richard A. Mathies
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Paper Abstract

Picosecond resonance Raman spectroscopy has been used to obtain structural information on the primary photointermediates of bacteriorhodopsin. A synchronously pumped dye laser was amplified at 50 Hz to produce a probe pulse at 589 nm. A second, spectrally distinct, pump pulse at 550 nm was generated by amplification of a 10 nm portion of a continuum produced from the probe pulse. This apparatus was used to record spectra of the J, K, and KL intermediates. The J spectrum exhibits strong hydrogen out-of-plane (HOOP) intensity and the fingerprint region consists of a broad series of lines centered at 1180 cm-1. By 3 ps, K has formed and the relative HOOP intensity decreases while the fingerprint collapses to a single mode at 1190 cm-1, characteristic of a 13-cis chromophore. These results argue that J contains a highly twisted chromophore which relaxes upon conversion to K and that isomerization is complete within 3 ps. Between 3 ps and 3.7 ns there is a resurgence in HOOP intensity and the ethylenic frequency rises from 1518 to 1521 cm-1 indicating the conversion of K to KL.

Paper Details

Date Published: 1 June 1991
PDF: 13 pages
Proc. SPIE 1432, Biomolecular Spectroscopy II, (1 June 1991); doi: 10.1117/12.44218
Show Author Affiliations
Stephen J. Doig, Univ. of California/Berkeley (United States)
Philip J. Reid, Univ. of California/Berkeley (United States)
Richard A. Mathies, Univ. of California/Berkeley (United States)


Published in SPIE Proceedings Vol. 1432:
Biomolecular Spectroscopy II
Robert R. Birge; Laurence A. Nafie, Editor(s)

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