Proceedings of the National Academy of Sciences · 2010 · 100 citations · 59 references
EngineeringHydrogen Bond BreakingBacteriophageMolecular BiologyRetinal ChromophoreComputational ChemistryElectronic Excited StateMolecular DynamicsDouble Bicycle-pedal IsomerizationProtein FoldingMolecular SimulationComputational BiochemistryPhotophysical PropertyBiophysicsBiochemistryMechanistic PhotochemistryProkaryotic VirusQuantum ChemistryPhotocycle Intermediate K.Excited State PropertyConical IntersectionNatural SciencesBacteriorhodopsin ProtonQuantum BiologyMolecular Biophysics
Quantum mechanics/molecular mechanics calculations based on ab initio multiconfigurational second order perturbation theory are employed to construct a computer model of Bacteriorhodopsin that reproduces the observed static and transient electronic spectra, the dipole moment changes, and the energy stored in the photocycle intermediate K. The computed reaction coordinate indicates that the isomerization of the retinal chromophore occurs via a complex motion accounting for three distinct regimes: (i) production of the excited state intermediate I, (ii) evolution of I toward a conical intersection between the excited state and the ground state, and (iii) formation of K. We show that, during stage ii, a space-saving mechanism dominated by an asynchronous double bicycle-pedal deformation of the C10═C11─C12═C13─C14═N moiety of the chromophore dominates the isomerization. On this same stage a N─H/water hydrogen bond is weakened and initiates a breaking process that is completed during stage iii.
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James P. Finley, Per‐Åke Malmqvist, Björn O. Roos et al. · Chemical Physics Letters · 1998 · 1.5K citations
Structure of bacteriorhodopsin at 1.55 Å resolution
Hartmut Luecke, Brigitte Schobert, Hans-Thomas Richter et al. · Journal of Molecular Biology · 1999 · 1.5K citations