Structural studies on dicopper(II) compounds with catechol oxidase activity

The X-ray crystal structures of three low molecular weight models of catechol oxidase with three different coordination modes are reported; and the compound with a bridging catecholate is shown to be the catalytically most active form.

[1]  Heinz Decker,et al.  Wie funktioniert die Tyrosinase? Neue Einblicke aus Modellchemie und Strukturbiologie , 2000 .

[2]  E. Monzani,et al.  Mechanistic, Structural, and Spectroscopic Studies on the Catecholase Activity of a Dinuclear Copper Complex by Dioxygen , 1999 .

[3]  M. Beltramini,et al.  The enzymatic properties of Octopus vulgaris hemocyanin: o-diphenol oxidase activity. , 1998, Biochemistry.

[4]  K. V. van Holde,et al.  Crystal structure of a functional unit from Octopus hemocyanin. , 1998, Journal of molecular biology.

[5]  E. Monzani,et al.  Tyrosinase Models. Synthesis, Structure, Catechol Oxidase Activity, and Phenol Monooxygenase Activity of a Dinuclear Copper Complex Derived from a Triamino Pentabenzimidazole Ligand. , 1998, Inorganic chemistry.

[6]  K. Karlin,et al.  Kinetics and Thermodynamics of Copper(I)/Dioxygen Interaction , 1997 .

[7]  E. Spodine,et al.  Oxidation of 3,5-ditert-butylcatechol catalyzed by copper(II) complexes. A kinetic study , 1997 .

[8]  E. Solomon,et al.  Multicopper Oxidases and Oxygenases. , 1996, Chemical reviews.

[9]  Bart Hazes,et al.  Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences , 1994, Proteins.

[10]  W G Hol,et al.  Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution. , 1994, Journal of molecular biology.

[11]  K. Karlin,et al.  Catecholate coordination to copper: structural characterization of a tetrachloro-o-catecholate-bridged dicopper(II) complex as a model for intermediates in copper-catalyzed oxidation of catechols , 1985 .

[12]  W. Hol,et al.  3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin , 1984, Nature.