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Science 8 February 1991:
Vol. 251. no. 4994, pp. 662 - 665
DOI: 10.1126/science.1992518
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Articles

Science, Vol 251, Issue 4994, 662-665
Copyright © 1991 by American Association for the Advancement of Science

articles

Large protein-induced dipoles for a symmetric carotenoid in a photosynthetic antenna complex

DS Gottfried, MA Steffen, and SG Boxer

Department of Chemistry, Stanford University, CA 94305.

Unusually large electric field effects have been measured for the absorption spectra of carotenoids (spheroidene) in the B800-850 light-harvesting complex from the photosynthetic bacterium Rhodobacter sphaeroides. Quantitative analysis shows that the difference in the permanent dipole moment between the ground state and excited states in this protein complex is substantially larger than for pure spheroidene extracted from the protein. The results demonstrate the presence of a large perturbation on the electronic structure of this nearly symmetric carotenoid due to the organized environment in the protein. This work also provides an explanation for the seemingly anomalous dependence of carotenoid band shifts on transmembrane potential and a generally useful approach for calibrating electric field-sensitive dyes that are widely used to probe potentials in biological systems.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Activation of Zeaxanthin Is an Obligatory Event in the Regulation of Photosynthetic Light Harvesting.
A. V. Ruban, A. A. Pascal, B. Robert, and P. Horton (2002)
J. Biol. Chem. 277, 7785-7789
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