Copper monooxygenase enzymes have been the focus of intense research due to the highly selective hydroxylation of unactivated substrates, including the strong C-H bond of methane. In the specific case of dopamine β-monooxygenase (DβM) and peptidylglycine α-hydroxylating monooxygenase (PHM), additional interest arises from the methionine-based thioether donor in the active site, which does not undergo sulfoxidation. In this context, we have reported that thioether modulation of the Cu<sup>2+</sup>/Cu<sup>+</sup> redox couple may include redox assistance to the metal center by an incipient sulfur radical cation character, and also a hemilabile character of the thioether moiety. The synthesis of novel thio- and selenoether-supported tripodal complexes has provided us fresh insight on the role of the soft S and Se donors (Fig. 1), and their potential relevance to the active sites of DβM and PHM. Spectroscopic characterization was complemented by reactivity studies, which are consistent with intra- and intermolecular H-abstraction in the rate-determining step.

Reactive copper-oxygen species with mixed benzimidazole/thio- and selenoether platforms relevant to the active site of PHM

251st National Meeting (2016)

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