title: What are the structural features of the active site that define binuclear copper proteins function?
abstract: The structural basis that define the physiological functions of binuclear copper enzymes is discussed in the frame of the data generated by a broad spectroscopic approach, spanning from paramagnetic NMR and pulsed EPR to x-ray absorption spectroscopies. The structural features discussed for the different oxidation and ligation states accessible to a binuclear copper sites are the coordination geometry for the first and second shell, the metal-metal distance and the role of the bridging exogenous ligand(s). A structural model will be presented to rationalize both the differentiation in function within the protein families and the reaction mechanism of those proteins that are enzymatically active.
authors.affiliation: Dipartimento di Biologia, Università degli studi di Padova, Padova, Italy.
authors.forename: Luigi
authors.initials: L
authors.lastname: Bubacco
authors.forename: Maurice
authors.initials: M
authors.lastname: van Gastel
authors.forename: Maurizio
authors.initials: M
authors.lastname: Benfatto
authors.forename: Armand W J W
authors.initials: AW
authors.lastname: Tepper
authors.forename: Gerard W
authors.initials: GW
authors.lastname: Canters
mesh_terms: D000818:Animals; D001665:Binding Sites; D003300:Copper / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D006433:Hemocyanins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D014442:Monophenol Monooxygenase / Q000737:chemistry*
chemical_list: D003300:Copper; D006433:Hemocyanins; D014442:Monophenol Monooxygenase