title: Electronic structure and its relation to function in copper proteins.
abstract: Spectroscopic and theoretical investigations of the geometric and electronic structures of mononuclear and binuclear copper sites in proteins help in understanding the contributions of these proteins to biological electron transfer. Spectroscopically calibrated density functional theory calculations, which give reasonable bonding descriptions in both ground- and excited-states, define the role of the protein in determining the geometric and electronic structure of the active site.
authors.affiliation: Department of Chemistry, Stanford University, Stanford, CA 94305, USA.
authors.forename: Robert K
authors.initials: RK
authors.lastname: Szilagyi
authors.forename: Edward I
authors.initials: EI
authors.lastname: Solomon
mesh_terms: D001665:Binding Sites; D003300:Copper / Q000737:chemistry*; D004583:Electrons; D008667:Metalloproteins / Q000737:chemistry*; D008958:Models, Molecular; D011789:Quantum Theory; D013057:Spectrum Analysis
chemical_list: D008667:Metalloproteins; D003300:Copper