The function of the metalloenzyme peptide deformylase (PDF) is to deformylate proteins that contain N-formylated methionine. Since this deformylation sequence is unique to prokaryotes, understanding the detailed mechanism of PDF may be important in the development of new antibiotics. In addition, further motivation for studying the mechanism comes from the unusual finding that the most active form of PDF is not a zinc-containing enzyme but instead an iron-containing enzyme. In order to explain the unusual metal dependency, we have prepared three new [N2S] ligands, which have been shown by X-ray crystallography to form mononuclear metal complexes. These [N2S] ligands model the cysteine and two histidine binding motif present in the active site of PDF. Details of the synthetic procedures, characterization data and reactivity of our complexes will be presented.

Structural modeling of peptide deformylase

239th National Meeting (2010)

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