Picosecond time-resolved resonance Raman spectroscopy of bacteriorhodopsin: structure and kinetics of the J, K, and KL intermediates

Stephen J. Doig; Philip J. Reid; Richard A. Mathies

doi:10.1117/12.44218

1 June 1991 Picosecond time-resolved resonance Raman spectroscopy of bacteriorhodopsin: structure and kinetics of the J, K, and KL intermediates

Stephen J. Doig, Philip J. Reid, Richard A. Mathies

Author Affiliations +

Proceedings Volume 1432, Biomolecular Spectroscopy II; (1991) https://doi.org/10.1117/12.44218
Event: Optics, Electro-Optics, and Laser Applications in Science and Engineering, 1991, Los Angeles, CA, United States

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.

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Stephen J. Doig, Philip J. Reid, and Richard A. Mathies "Picosecond time-resolved resonance Raman spectroscopy of bacteriorhodopsin: structure and kinetics of the J, K, and KL intermediates", Proc. SPIE 1432, Biomolecular Spectroscopy II, (1 June 1991); https://doi.org/10.1117/12.44218

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