Urease is the most efficient enzyme known to date, and this efficiency relies on the presence of an active site containing two Ni(II) ions. The structural properties of the enzyme in the native state and in complex with several inhibitors have been the focus of our studies in the past several years. Recently, we determined the structural and kinetic determinants of urease inhibition by fluoride, dimethylsulphoxide, phosphite and other small molecules. These results shed new light on the chemistry of the metal ions in the active site of the enzyme.

New insights in the chemistry of nickel in urease

249th National Meeting (2015)

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