Electronic Structure of the Reduced Blue Copper Active Site: Contributions to Reduction Potentials and Geometry

Abstract

A detailed electronic structure description of the reduced blue copper active site has now been developed. Photoelectron spectroscopy (PES) of imidazole, dimethyl sulfide, and methanethiolate bound to Cu(I) sites at single crystal surfaces has been used to define normal Cu(I) bonding to ligands relevant to the blue copper site. Variable photon energy PES has been used to assign valence band spectra, assess metal-ligand covalency, and probe specific orbital contributions to Cu(I) bonding. Self Consistent Field-X{alpha}-Scattered Wave (SCF-X{alpha}-SW) molecular orbital calculations calibrated to the photoelectron spectra have been performed to quantitatively complement the experimental bonding descriptions. These calculations have been extended to the reduced blue copper active site in plastocyanin, the prototypical blue copper protein, to detail the electronic structure changes that occur relative to normal Cu(I) bonding and upon oxidation. Ionization energies have been used to estimate the electronic structure contributions to the reduction potential. The long Cu-thioether axial bond present at the active site destabilizes the oxidized state and is therefore a key determining factor in the high reduction potentials generally observed for blue copper proteins. Linear coupling terms have been evaluated for the distortions of a blue copper site unconstrained by the protein backbone. 99 refs., 22 figs.,more » 12 tabs.« less