My work is centered on delineating the mechanisms according to which metalloproteins involved in processes essential for life perform the activation of small (or larger) molecules, how the specific identity of the metals in the active sites allows their chemical diversion and selectivity and what the functional role of iron-sulfur clusters in proteins involved in DNA synthesis and repair is. The research of the group revolves around proteins that are candidates to be the targets of new antiviral factors and to mediate DNA modifications and other important chemical transformations. These proteins often belong to large structural superfamilies with apparently similar representatives that are carrying out radically different reactions. We want to understand those functions and the extant determinants that endow this chemical versatility.