文摘
2003 marked a banner year in the bioinorganic chemistry of mononuclear non-heme iron enzymes. The first non-heme oxoiron(IV) intermediate (called J) was trapped and characterized by Bollinger and Krebs in the catalytic cycle of taurine dioxygenase (TauD), and the first crystal structure of a synthetic non-heme oxoiron(IV) complex was reported by M眉nck, Nam, and Que. These results stimulated inorganic chemists to synthesize related oxoiron(IV) complexes to shed light on the electronic structures and spectroscopic properties of these novel intermediates and gain mechanistic insights into their function in biology. All of the biological oxoiron(IV) intermediates discovered since 2003 have an S = 2 ground spin state, while over 90% of the 60 or so synthetic oxoiron(IV) complexes reported to date have an S = 1 ground spin state. This difference in electronic structure has fueled an interest to more accurately model these enzymatic intermediates and synthesize S = 2 oxoiron(IV) complexes.