A Synthetic Molybdenum Complex that Mimics All Four Molybdopterin Enzyme Families and Enables Catalytic C–H Oxidation

Le résumé fourni par la source

Molybdopterin enzymes catalyze a remarkably diverse array of redox transformations, ranging from oxyanion reduction to C–H hydroxylation, through MoVI/MoIV cycling at active sites with conserved dithiolate-coordinated structures. Synthetic models of these active sites have historically struggled to replicate this chemical versatility in part due to comproportionation to inactive MoV dimers, and catalytic turnover remains elusive. Here we report that a [N2S2]2–-supported MoIV=O complex abstracts oxygen atoms from substrates representative of three molybdopterin enzyme families: DMSO, trimethylamine N-oxide, perchlorate, nitrate, and selenate (DMSO reductases); methionine sulfoxide (sulfite oxidases); and benzamidoxime and N-hydroxyphthalimide (mARCs). In the cases of ClO4– and NO3–, efficient oxygen atom transfer (OAT) requires Lewis acid activation by B(C6F5)3. The corresponding MoVI(O)2 redox partner oxidizes formate via hydride abstraction, extending the functional analogy to formate dehydrogenases. The same complex has previously been shown to promote C–H hydroxylation by hydride abstraction akin to the XO family, thus demonstrating

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