title: Theoretical study of oxyhemocyanin active site: a possible insight on the first step of phenol oxidation by tyrosinase.
abstract: Extended Huckel theory calculations have been carried out on a model of the oxyhemocyanin active site that includes six imidazoles, the two copper cations, and a dioxygen molecule. The results obtained for the very likely mu-eta 2:eta 2 arrangement of the dioxygen molecule show that the most favorable orientation of O2 is such that the two long Cu-N coordination bonds are perpendicular to the plane formed by the two metal atoms and O2. This arrangement leads to pentacoordinated coppers with a distorted square pyramidal geometry. The molecular electrostatic potential maps of the complexes exhibit a potential well located close to the peroxo anion midbond. The dependence of the energy and of the molecular electrostatic maps on the precise orientation and location of the imidazole rings has been investigated. These results, which show the important role played by the third remote imidazole ligand, are discussed in relation with the first step of tyrosinase-mediated phenol oxidation.
authors.affiliation: Laboratoire de Chimie Théorique, Université de Paris Sud, Orsay, France.
authors.forename: O
authors.initials: O
authors.lastname: Eisenstein
authors.forename: C
authors.initials: C
authors.lastname: Giessner-Prettre
authors.forename: J
authors.initials: J
authors.lastname: Maddaluno
authors.forename: D
authors.initials: D
authors.lastname: Stussi
authors.forename: J
authors.initials: J
authors.lastname: Weber
mesh_terms: D001665:Binding Sites; D002151:Calorimetry; D004563:Electrochemistry; D006433:Hemocyanins / Q000737:chemistry* / Q000378:metabolism; D007093:Imidazoles / Q000737:chemistry; D008433:Mathematics; D008958:Models, Molecular; D008962:Models, Theoretical; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010636:Phenols / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D007093:Imidazoles; D010636:Phenols; C021724:oxy-beta-hemocyanin; D006433:Hemocyanins; D014442:Monophenol Monooxygenase