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Science 16 June 1978:
Vol. 200. no. 4347, pp. 1279 - 1281
DOI: 10.1126/science.663607
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Articles

Science, Vol 200, Issue 4347, 1279-1281
Copyright © 1978 by American Association for the Advancement of Science

articles

Subpicosecond spectroscopy of bacteriorhodopsin

EP Ippen, CV Shank, A Lewis, and MA Marcus

Subpicosecond pulses have been used to study the ultrafast dynamics of the photochemistry of bacteriorhodopsin. An optically induced absorption that appears in about 1.0 picosecond at physiological temperatures has been resolved in time. The data can be interpreted in terms of the photochemical formation of bathobacteriorhodopsin and provide support for an excitation mechanisms involving molecular rearrangement in the protein induced by electron redistribution in the chromophore.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Bioenergetics of the Archaea.
G. Schafer, M. Engelhard, and V. Muller (1999)
Microbiol. Mol. Biol. Rev. 63, 570-620
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Direct observation of the femtosecond excited-state cis-trans isomerization in bacteriorhodopsin.
R. Mathies, C. Brito Cruz, W. Pollard, and C. Shank (1988)
Science 240, 777-779
   Abstract »    PDF »
Picosecond chemical and biological events.
P. Rentzepis (1978)
Science 202, 174-182
   Abstract »    PDF »


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