Metalloproteins comprise almost one half of the known enzymes and promote catalytic processes essential for the human health and the environment. The focus of the lab is on metalloproteins that are targets for new antiviral/anticancer factors, mediate DNA modifications or perform challenging chemical transformations. The laboratory employs spectroscopic and transient kinetic techniques in tandem with structural biology and biochemical approaches to determine how transition metals confer their powerful reactivity to accomplish chemically challenging transformations in biology. In particular, we are interested to determine how transition metal reactivity is controlled by protein structure, to map the functional and structural repertoire of (un)known metalloproteins and to establish their molecular mechanisms. 

The systems of interest can be segregated into two categories:

a)   [Fe-S]-containing enzymes

b)   mono- or polynuclear metalloclusters of large protein superfamilies

c)   viral proteases