Ground state structures and electronic excitations of biological chromophores at Quantum Monte Carlo/Many Body Green’s Function Theory level

Abstract

The accurate calculation of electronic excited states of large and electronically correlated biological chromophores in their complex protein environment still represents a challenge for quantum chemistry. Two ab initio techniques are recently emerging as candidates to correctly tackle this issue: Quantum Monte Carlo (QMC) calculations for the ground state geometry optimization, and Many Body Green’s Function Theory (MBGFT) for exited state energies. In the present work we use the Variational Monte Carlo (VMC) to carry out structural optimizations and we present an extension of MBGFT to complex environments, using a Quantum Mechanics/Molecular Mechanics framework. This technique is applied to evaluate the optical properties of the retinal protonated Schiff base (RPSB) chromophore in rhodopsin, the protein responsible for dim light vision in the vertebrates. Vertical energies for the bright excitation of RPSB calculated solving the Bethe–Salpeter equation in gas phase and in the protein environment correspond to 2.19eV and 2.58eV, respectively. These data are in fair agreement with the available experimental findings. The comparison between these excitation energies and that obtained for a gas phase calculation on a retinal geometry obtained in the protein environment (2.03eV) reveals the essential role of the protein field in the spectral tuning of the molecule. The proposed VMC/MBGFT methodologies can therefore be applied to obtain a reliable ab initio evaluation of optical properties of biological chromophores.