A molecular spring for vision.

Details

Serval ID
serval:BIB_5ED654591B81
Type
Article: article from journal or magazin.
Collection
Publications
Title
A molecular spring for vision.
Journal
Journal of the American Chemical Society
Author(s)
Röhrig U.F., Guidoni L., Laio A., Frank I., Rothlisberger U.
ISSN
0002-7863 (Print)
ISSN-L
0002-7863
Publication state
Published
Issued date
2004
Peer-reviewed
Oui
Volume
126
Number
47
Pages
15328-15329
Language
english
Abstract
Light absorption by the visual pigment rhodopsin leads to vision via a complex signal transduction pathway that is initiated by the ultrafast and highly efficient photoreaction of its chromophore, the retinal protonated Schiff base (RPSB). Here, we investigate this reaction in real time by means of unrestrained molecular dynamics simulations of the protein in a membrane mimetic environment, treating the chromophore at the density functional theory level. We demonstrate that a highly strained all-trans RPSB is formed starting from the 11-cis configuration (dark state) within approximately 100 fs by a minor rearrangement of the nuclei under preservation of the saltbridge with Glu113 and virtually no deformation of the binding pocket. Hence, the initial step of vision can be understood as the compression of a molecular spring by a minor change of the nuclear coordinates. This spring can then release its strain by altering the protein environment.
Keywords
Algorithms, Models, Molecular, Photochemistry, Protein Binding, Quantum Theory, Receptors, G-Protein-Coupled/chemistry, Receptors, G-Protein-Coupled/metabolism, Retinaldehyde/chemistry, Retinaldehyde/metabolism, Rhodopsin/chemistry, Rhodopsin/metabolism, Schiff Bases/chemistry, Schiff Bases/metabolism, Thermodynamics
Pubmed
Web of science
Create date
30/10/2015 9:01
Last modification date
20/08/2019 14:16
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