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• W3089838238 endingPage "12255" @default.
• W3089838238 startingPage "12239" @default.
• W3089838238 abstract "Iron is an especially important redox-active cofactor in biology because of its ability to mediate reactions with atmospheric O2. Iron-dependent oxygenases exploit this earth-abundant transition metal for the insertion of oxygen atoms into organic compounds. Throughout the astounding diversity of transformations catalyzed by these enzymes, the protein framework directs reactive intermediates toward the precise formation of products, which, in many cases, necessitates the cleavage of strong C-H bonds. In recent years, members of several iron-dependent oxygenase families have been engineered for new-to-nature transformations that offer advantages over conventional synthetic methods. In this Perspective, we first explore what is known about the reactivity of heme-dependent cytochrome P450 oxygenases and nonheme iron-dependent oxygenases bearing the 2-His-1-carboxylate facial triad by reviewing mechanistic studies with an emphasis on how the protein scaffold maximizes the catalytic potential of the iron-heme and iron cofactors. We then review how these cofactors have been repurposed for abiological transformations by engineering the protein frameworks of these enzymes. Finally, we discuss contemporary challenges associated with engineering these platforms and comment on their roles in biocatalysis moving forward." @default.
• W3089838238 created "2020-10-08" @default.
• W3089838238 creator A5028465253 @default.
• W3089838238 creator A5033526989 @default.
• W3089838238 date "2020-09-28" @default.
• W3089838238 modified "2023-10-17" @default.
• W3089838238 title "Nature’s Machinery, Repurposed: Expanding the Repertoire of Iron-Dependent Oxygenases" @default.
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