ArticleJournal of the American Chemical Society2024
Myoglobin-Catalyzed Azide Reduction Proceeds via an Anionic Metal Amide Intermediate.
Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Engineering Enantiocomplementary Protoglobins for Stereoconvergent Construction ofJournal of the American Chemical Society · 2026Article
- Uncertainty Quantification forChemical reviews · 2026Review
- High-Throughput Screening of Co-Protoporphyrin IX-Binding Proteins for Enhanced Hydrogen Production.Molecules (Basel, Switzerland) · 2026Article
- Is a Malleable Active Site Loop the Key to High Substrate Promiscuity? Hybrid, Biocatalytic Route to Structurally Diverse Taxoid Side Chains with Remarkable Dual Stereocontrol.Angewandte Chemie (International ed. in English) · 2025Article
- A new heme enzyme family forms hydrazine groups in diverse biosynthetic pathways.bioRxiv : the preprint server for biology · 2025Article
- Metal Complexes of Bispidine Derivatives: Achievements and Prospects for the Future.Molecules (Basel, Switzerland) · 2025Review
- Catalyzing the future: recent advances in chemical synthesis using enzymes.Current opinion in chemical biology · 2024Review
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nitrene transfer reactions catalyzed by heme proteins have broad potential for the stereoselective formation of carbon-nitrogen bonds. However, competition between productive nitrene transfer and the undesirable reduction of nitrene precursors limits the broad implementation of such biocatalytic methods. Here, we investigated the reduction of azides by the model heme protein myoglobin to gain mechanistic insights into the factors that control the fate of key reaction intermediates. In this system, the reaction proceeds via a proposed nitrene intermediate that is rapidly reduced and protonated to give a reactive ferrous amide species, which we characterized by UV/vis and Mössbauer spectroscopies, quantum mechanical calculations, and X-ray crystallography. Rate-limiting protonation of the ferrous amide to produce the corresponding amine is the final step in the catalytic cycle. These findings contribute to our understanding of the heme protein-catalyzed reduction of azides and provide a guide for future enzyme engineering campaigns to create more efficient nitrene transferases. Moreover, harnessing the reduction reaction in a chemoenzymatic cascade provided a potentially practical route to substituted pyrroles.
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Registered trials
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