Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 20 March 1998:
Vol. 279. no. 5358, pp. 1886 - 1891
DOI: 10.1126/science.279.5358.1886
Prev | Table of Contents | Next

Articles

Chemical Dynamics in Proteins: The Photoisomerization of Retinal in Bacteriorhodopsin

Feng Gai, * K. C. Hasson, dagger J. Cooper McDonald, Philip A. Anfinrud ddagger

Chemical dynamics in proteins are discussed, with bacteriorhodopsin serving as a model system. Ultrafast time-resolved methods used to probe the chemical dynamics of retinal photoisomerization in bacteriorhodopsin are discussed, along with future prospects for ultrafast time-resolved crystallography. The photoisomerization of retinal in bacteriorhodopsin is far more selective and efficient than in solution, the origins of which are discussed in the context of a three-state model for the photoisomerization reaction coordinate. The chemical dynamics are complex, with the excited-state relaxation exhibiting a multiexponential decay with well-defined rate constants. Possible origins for the two major components are also discussed.

The authors are in the Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA.
*   Present address: Los Alamos National Laboratory, CST-4, MS J586, Los Alamos, NM 87545, USA.

dagger    Present address: Magnetic Imaging Technologies, 2500 Meridian Parkway, Suite 175, Durham, NC 27713, USA.

ddagger    To whom correspondence should be addressed. E-mail: anfinrud{at}chemistry.harvard.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Control of retinal isomerization in bacteriorhodopsin in the high-intensity regime.
A. C. Florean, D. Cardoza, J. L. White, J. K. Lanyi, R. J. Sension, and P. H. Bucksbaum (2009)
PNAS 106, 10896-10900
   Abstract »    Full Text »    PDF »
Coherent control of retinal isomerization in bacteriorhodopsin..
V. I. Prokhorenko, A. M. Nagy, S. A. Waschuk, L. S. Brown, R. R. Birge, and R. J. D. Miller (2006)
Science 313, 1257-1261
   Abstract »    Full Text »    PDF »
Insights into excited-state and isomerization dynamics of bacteriorhodopsin from ultrafast transient UV absorption..
S. Schenkl, F. van Mourik, N. Friedman, M. Sheves, R. Schlesinger, S. Haacke, and M. Chergui (2006)
PNAS 103, 4101-4106
   Abstract »    Full Text »    PDF »
From The Cover: The retinal chromophore/chloride ion pair: Structure of the photoisomerization path and interplay of charge transfer and covalent states.
A. Cembran, F. Bernardi, M. Olivucci, and M. Garavelli (2005)
PNAS 102, 6255-6260
   Abstract »    Full Text »    PDF »
Deformation of Helix C in the Low Temperature L-intermediate of Bacteriorhodopsin.
K. Edman, A. Royant, G. Larsson, F. Jacobson, T. Taylor, D. van der Spoel, E. M. Landau, E. Pebay-Peyroula, and R. Neutze (2004)
J. Biol. Chem. 279, 2147-2158
   Abstract »    Full Text »    PDF »
Photoexcited breathers in conjugated polyenes: An excited-state molecular dynamics study.
S. Tretiak, A. Saxena, R. L. Martin, and A. R. Bishop (2003)
PNAS 100, 2185-2190
   Abstract »    Full Text »    PDF »
Femtosecond Infrared Spectroscopy of Bacteriorhodopsin Chromophore Isomerization.
J. Herbst, K. Heyne, and R. Diller (2002)
Science 297, 822-825
   Abstract »    Full Text »    PDF »
The relaxation dynamics of the excited electronic states of retinal in bacteriorhodopsin by two-pump-probe femtosecond studies.
S. L. Logunov, V. V. Volkov, M. Braun, and M. A. El-Sayed (2001)
PNAS
   Abstract »    Full Text »    PDF »
An unusual pathway of excitation energy deactivation in carotenoids: Singlet-to-triplet conversion on an ultrafast timescale in a photosynthetic antenna.
C. C. Gradinaru, J. T. M. Kennis, E. Papagiannakis, I. H. M. van Stokkum, R. J. Cogdell, G. R. Fleming, R. A. Niederman, and R. van Grondelle (2001)
PNAS
   Abstract »    Full Text »
Computational evidence in favor of a two-state, two-mode model of the retinal chromophore photoisomerization.
R. Gonzalez-Luque, M. Garavelli, F. Bernardi, M. Merchan, M. A. Robb, and M. Olivucci (2000)
PNAS 97, 9379-9384
   Abstract »    Full Text »    PDF »
Femtochemistry.
Y. Tanimura, K. Yamashita, and P. A. Anfinrud (1999)
PNAS 96, 8823-8824
   Abstract »    Full Text »    PDF »
Shedding light on the dark and weakly fluorescent states of green fluorescent proteins.
W. Weber, V. Helms, J. A. McCammon, and P. W. Langhoff (1999)
PNAS 96, 6177-6182
   Abstract »    Full Text »    PDF »
An unusual pathway of excitation energy deactivation in carotenoids: Singlet-to-triplet conversion on an ultrafast timescale in a photosynthetic antenna.
C. C. Gradinaru, J. T. M. Kennis, E. Papagiannakis, I. H. M. van Stokkum, R. J. Cogdell, G. R. Fleming, R. A. Niederman, and R. van Grondelle (2001)
PNAS 98, 2364-2369
   Abstract »    Full Text »    PDF »
The relaxation dynamics of the excited electronic states of retinal in bacteriorhodopsin by two-pump-probe femtosecond studies.
S. L. Logunov, V. V. Volkov, M. Braun, and M. A. El-Sayed (2001)
PNAS 98, 8475-8479
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)