The function of the metalloenzyme peptide deformylase (PDF) is to deformylate proteins that contain N-formylated methionine. Our interest in studying PDF stems from the unusual finding that the most active form of PDF contains a different metal than previously hypothesized. Initially, it was predicted that the metal ion contained zinc but recently it was discovered that iron is utilized instead. This unusual metal dependency on PDF activity is hypothesized to be link to the different geometric coordination preferences of iron versus zinc (i.e. Zn prefers to be four-coordinate and Fe five-coordinate). In order to test this hypothesis, we have prepared Zn and Cd compounds that are complexed by a N2S ligand that is designed to mimic the two histidine and cysteine amino acid residues that bind the metal ion in the active site of PDF. Details of the synthetic procedures, characterization data and reactivity of our complexes will be presented.

Investigation of the unusual metal dependency of peptide deformylase using Zn(II) and Cd(II) synthetic model complexes

247th National Meeting (2014)

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