Dioxygen Binds End-on to Mononuclear Copper in a Precatalytic Enzyme Complex

Copper active sites play a major role in enzymatic activation of dioxygen. We trapped the copper-dioxygen complex in the enzyme peptidylglycine-alpha-hydroxylating monooxygenase (PHM) by freezing protein crystals that had been soaked with a slow substrate and ascorbate in the presence of oxygen. The...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 2004-05, Vol.304 (5672), p.864-867
Hauptverfasser:	Prigge, Sean T., Eipper, Betty A., Mains, Richard E., Amzel, L. Mario
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Atoms Binding Sites Biological and medical sciences Catalysis CATALYSTS Catalytic Domain CHEMICAL BONDS COPPER Copper - metabolism Crystal structure Crystalline structure Crystallization Crystallography, X-Ray Crystals Dipeptides - chemistry Dipeptides - metabolism Electron density Electron transfer Electron Transport Enzyme kinetics ENZYMES Fundamental and applied biological sciences. Psychology Glycine - chemistry Glycine - metabolism Hydrogen Hydrogen - metabolism Hydrogen Bonding Hydrogen bonds INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY Kinetics Ligands Mixed Function Oxygenases - chemistry Mixed Function Oxygenases - metabolism Models, Molecular Molecular biophysics Multienzyme Complexes - chemistry Multienzyme Complexes - metabolism NATIONAL SYNCHROTRON LIGHT SOURCE Oxidation-Reduction OXYGEN Oxygen - metabolism Peptides Peptides - metabolism Protein Conformation Rats Structure in molecular biology Water - metabolism
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