Protein Induced Torsion of the Retinal Chromophore and How it Affects the Photochemistry of Rhopdopsin

Journal Article · Wed Dec 26 00:00:00 EST 2007 · AIP Conference Proceedings

DOI:https://doi.org/10.1063/1.2836175· OSTI ID:21043542

Weingart, Oliver; Buss, Volker ^[1]

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1. Theoretische Chemie, Universitaet Duisburg-Essen, Universitaetsstr. 2 D-45141 Essen (Germany)

The influence of protein induced chromophore deformations on reaction timescale and quantum yield is investigated using ab initio molecular dynamics in vacuo on four and five double bond models of the retinal chromophore. The opposite twist of the C11 = C12 and the C12-C13 bonds appears to be the prerequisite for the highly stereoselective and efficient cis-trans photodynamics of the retinal chromophore in the binding pocket of rhodopsin. The formation of the photoproduct is determined by the phase of the hydrogen out-of-plane mode of the 11-cis double bond.

• OSTI ID: 21043542
• Journal Information: AIP Conference Proceedings, Vol. 963, Issue 2; Conference: ICCMSE 2007: International conference on computational methods in science and engineering, Corfu (Greece), 25-30 Sep 2007; Other Information: DOI: 10.1063/1.2836175; (c) 2007 American Institute of Physics; Country of input: International Atomic Energy Agency (IAEA); ISSN 0094-243X
• Country of Publication: United States
• Language: English

Related Subjects

74 ATOMIC AND MOLECULAR PHYSICS
CHEMICAL BONDS
DEFORMATION
EXCITED STATES
HYDROGEN
MOLECULAR DYNAMICS METHOD
PHOTOCHEMISTRY
RHODOPSIN
TORSION