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The design of metal-binding sites in proteins that combine high affinity with high selectivity for the desired metal ion remains a challenging goal. Recently, a protein designed to display femtomolar affinity forUO    2    2  +, dubbed “Super Uranyl-binding Protein” (SUP), was described, with potential applications for removingUO    2    2  +in water. Although it discriminated most metal ions present in seawater, the protein showed a surprisingly high affinity for Cu 2+  ions. Here, we have investigated Cu 2+  binding to SUP using a combination of electron paramagnetic resonance, fluorescence and circular dichroism spectroscopies. Our results provide evidence for two Cu 2+  binding sites on SUP that are distinct from theUO    2    2  +binding site, but one of which interferes withUO    2    2  +binding. They further suggest that in solution the protein's secondary structure changes significantly in response to bindingUO    2    2  +; in contrast, the crystal structures of the apo- and holo-protein are almost superimposable. These results provide insights for further improving the selectivity of SUP forUO    2    2  +, paving the way toward protein-based biomaterials for decontamination and/or recovery of uranium.

Probing Metal Ion Discrimination in a Protein Designed to Bind Uranyl Cation With Femtomolar Affinity