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Conferences > UP > 1996 > PDP > PDP.5

A Comparative Study of the Initial Photoinduced Event in Bacteriorhodopsin: Can it be Isomerization?

Q. Zhong, S. Ruhman, M. Ottolenghi, M. Sheves, N. Friedman, G.H. Atkinson, and J.K. Delaney

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Abstract

Rhodopsins are a family of photoactivated 7 α-helix membrane proteins which play central roles in visual-transduction and bacterial photosynthesis. They share the same chromophore: A retinal polyene bound to the protein via a protonated Schiff base linkage. A comprehensive description of the molecular mechanism of light energy conversion in rhodopsins requires a detailed understanding of the primary photophysical events.

© 1996 Optical Society of America

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