Bubacco Luigi, van Gastel Maurice, Benfatto Maurizio, Tepper Armand W J W, Canters Gerard W
Dipartimento di Biologia, Università degli studi di Padova, Padova, Italy.
Micron. 2004;35(1-2):143-5. doi: 10.1016/j.micron.2003.10.046.
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.
