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Originally published as Biophys J. BioFAST on April 20, 2007.
doi:10.1529/biophysj.107.108225
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Biophysical Journal 92:L106-L108 (2007)
© 2007 The Biophysical Society

Photoisomerization Mechanism of Rhodopsin and 9-cis-Rhodopsin Revealed by X-ray Crystallography

Hitoshi Nakamichi *, Volker Buss {dagger} and Tetsuji Okada *

* Biological Information Research Center, National Institute of Advanced Industrial Science and Technology, Tokyo, Japan; and {dagger} Department of Chemistry, University of Duisburg-Essen, Duisburg, Germany

Correspondence: Address reprint requests and inquiries to Tetsuji Okada, Tel.: 81-3-3599-8562; Fax: 81-3-3599-8562; E-mail: t-okada{at}aist.go.jp.

The primary photochemical process of the visual function has been investigated using the three crystallographic models, 11-cis-rhodopsin, all-trans-bathorhodopsin, and the artificial isomeric 9-cis-rhodopsin. Detailed examination of the atomic displacements and dihedral angle changes of the retinal chromophore involved in the interconversion among these isomers suggests the mechanism of isomerization efficiency.







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Copyright © 2007 by the Biophysical Society.