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Theoretical Chemistry Accounts

, Volume 109, Issue 3, pp 125–132 | Cite as

Investigation of the S0S1 excitation in bacteriorhodopsin with the ONIOM(MO:MM) hybrid method

  • T. Vreven
  • K. Morokuma
Regular article

Abstract.

 We have investigated the S0 and S1 electronic states in bacteriorhodopsin using a variety of QM/MM levels. The decomposition of the calculated excitation energies into electronic and electrostatic components shows that the interaction of the chromophore with the protein electric field increases the excitation energy, while polarization effects are negligible. Therefore, the experimentally observed reduction in excitation energy from solution phase to protein environment (the Opsin shift) does not come from the electrostatic interaction with the protein environment, but from either the interaction ofthe chromophore with the solvent or counter ion, or structural effects. Our high-level ONIOM(TD– B3LYP:Amber) calculation predicts the excitation energy within 8 kcal/mol from experiment, the discrepancy probably being caused by the neglect of polarization of the protein environment. In addition, we have shown that the level of optimization is extremely critical for the calculation of accurate excitation energies in bacteriorhodopsin.

Keywords: Opsin shift – Bacteriorhodopsin – ONIOM – QM/MM – Hybrid methods 

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Copyright information

© Springer-Verlag Berlin Heidelberg 2003

Authors and Affiliations

  • T. Vreven
    • 1
  • K. Morokuma
    • 1
  1. 1.Cherry L. Emerson Center for Scientific Computation and Department of Chemistry, Emory University, Atlanta, GA 30322, USAUS

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