Effective fragment potentials and spectroscopy at enzyme active sites.

Spectroscopy at a biochemical active site is influenced by local fields and hydrogen-bonds. Quantum calculations of the electronic structure of the entire biomolecule is, of course, impossible, but the chemical system can be modeled by dividing it into an active region (A) described quantum mechanically, and a spectator region (S) that influences A with strong fields and hydrogen-bonds. The all-electron interaction between A and S is replaced by an effective fragment potential (EFP) which represents the interaction as electrostatic, polarization and exchange repulsion terms. The EFP are derived entirely by ab initio model calculations of the S electronic properties and interactions and have been implemented in the quantum chemistry code, GAMESS. Spectroscopic analysis of enzyme active sites using the EFP will examine rhodanese and glutathione bound to glutathione S-transferase. The effect of specific hydrogen-bonds and local helices on spectral shifts is determined.