Simulation of the Effect of Reorientation of Hydrogen Bonds in Proteins on Long-Range Electron Transfer

We present Monte Carlo simulations illustrating the influence of reorientation of hydrogen bonds in proteins on long-range interprotein electron transfer. The lattice protein model employed mimics the electron donor (or acceptor) interacting with an antiparallel sheet. In addition, we take into account harmonic vibrations of the medium and also the dependence of the coupling matrix element on orientation of hydrogen bonds near the donor and/or acceptor. The results obtained show that the interaction between the tunneling electron and amino-acid residues, which are responsible for the formation of hydrogen bonds, may result in broadening the parabolic dependence of the electron-transfer rate constant on the reaction exothermicity and also in deviations from this dependence especially in the cases when the sheet is linked with the electron donor.