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Sulfur ligation in metalloenzymes often gives the active site unique properties, whether it is the axial cysteinate ligand in the cytochrome P450s or the equatorial sulfur/thiol ligation in nonheme iron enzymes. To understand sulfur ligation to iron complexes and how it affects the structural, spectroscopic, and intrinsic properties of the active species and the catalysis of substrates, we pursued a systematic study and compared sulfur with amine-ligated iron(IV)–oxo complexes. We synthesized and characterized a biomimetic N4S-ligated iron(IV)–oxo complex and compared the obtained results with an analogous N5-ligated iron(IV)–oxo complex. Our work shows that the amine for sulfur replacement in the equatorial ligand framework leads to a rate enhancement for oxygen atom and hydrogen atom transfer reactions. Moreover, the sulfur-ligated iron(IV)–oxo complex reacts through a different reaction mechanism as compared to the N5-ligated iron(IV)–oxo complex, where the former reacts through hydride transfer with the latter reacting via radical pathways. We show that the reactivity differences are caused by a dramatic change in redox potential between the two complexes. Our studies highlight the importance of implementing a sulfur ligand into the equatorial ligand framework of nonheme iron(IV)–oxo complexes and how it affects the physicochemical properties of the oxidant and its reactivity.
Satpathy et al. (Fri,) studied this question.