Cerium binding to proteins: a structural analysis

Ce-peptide and Ce-protein adducts can be used to improve stability, solubility, and distribution of Ce ions and Ce complexes within the body and to create artificial metalloenzymes with catalase and superoxide dismutase activities. However, the mechanisms by which Ce is recognized by proteins are not entirely known at the atomic level. Here, a comparative analysis of the few examples of known Ce/protein structures is presented and the results of this analysis are discussed. Ce 3+ can replace Ca 2+ and Ce 4+ can replace Fe 3+ . Ce ions are mainly located on the side chains of Asp and Glu (in both monodentate and bidentate binding modes) with a large variability in their coordination number. No major global structural rearrangement is apparent in the analyzed examples. However, the dataset used for the analysis is very limited. Thus, this perspective is intended to encourage further research in the field of Ce-protein interaction.