What are the structural features of the active site that define binuclear copper proteins function?
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.
Bubacco
Luigi
L
Dipartimento di Biologia, Università degli studi di Padova, Padova, Italy.
van Gastel
Maurice
M
Benfatto
Maurizio
M
Tepper
Armand W J W
AW
Canters
Gerard W
GW
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*
D003300:Copper; D006433:Hemocyanins; D014442:Monophenol Monooxygenase