ArticleBioorganic & medicinal chemistry2014
Intramolecular C(sp(3))H amination of arylsulfonyl azides with engineered and artificial myoglobin-based catalysts.
Article in Bioorganic & medicinal chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- Stereoselective Synthesis of Aminals Through Enzyme-Catalyzed Intermolecular C(spAngewandte Chemie (International ed. in English) · 2026Article
- Design-Evolution Synergy Enables New-to-Nature Enzyme Chemistry.bioRxiv : the preprint server for biology · 2026Article
- High-Throughput Screening of Co-Protoporphyrin IX-Binding Proteins for Enhanced Hydrogen Production.Molecules (Basel, Switzerland) · 2026Article
- Expanding the Terpene Universe: Synthetic Biology and Non-Natural Chemistry in Engineered Microorganisms.Molecules (Basel, Switzerland) · 2025Review
- Enzyme-catalyzed C(spRSC advances · 2025Article
- Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025Review
- Myoglobin-Catalyzed Azide Reduction Proceeds via an Anionic Metal Amide Intermediate.Journal of the American Chemical Society · 2024Article
- Stereoselective Construction of β-, γ-, and δ-Lactam Rings via Enzymatic C-H Amidation.Nature catalysis · 2024Article
- HowJACS Au · 2023Article
- Mechanistic manifold in a hemoprotein-catalyzed cyclopropanation reaction with diazoketone.Nature communications · 2023Article
- Directed Evolution of an Iron(II)- and α-Ketoglutarate-Dependent Dioxygenase for Site-Selective Azidation of Unactivated Aliphatic C-H Bonds.Angewandte Chemie (International ed. in English) · 2023Article
- Stereoselective Construction of β-, γ-, and δ-Lactam Rings via Enzymatic C-H Amidation.Research square · 2023Article
- Biocatalytic Intramolecular C-H aminations via Engineered Heme Proteins: Full Reaction Pathways and Axial Ligand Effects.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Engineered myoglobin as a catalyst for atom transfer radical cyclisation.Chemical communications (Cambridge, England) · 2022Article
- Peroxidase Activity of Myoglobin Variants Reconstituted with Artificial Cofactors.Chembiochem : a European journal of chemical biology · 2022Article
- Organometallic catalysis in aqueous and biological environments: harnessing the power of metal carbenes.Chemical science · 2022Review
- Corrole-protein interactions in H-NOX and HasA.RSC chemical biology · 2022Article
- Directed Evolution of Artificial Metalloenzymes in Whole Cells.Angewandte Chemie (International ed. in English) · 2022Article
- Assembly and Evolution of Artificial Metalloenzymes withinJournal of the American Chemical Society · 2022Article
- Engineered Myoglobin Catalysts for Asymmetric Intermolecular Cyclopropanation Reactions.Bulletin of Japan Society of Coordination Chemistry · 2022Article
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3 authors.
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Abstract
The direct conversion of aliphatic CH bonds into CN bonds provides an attractive approach to the introduction of nitrogen-containing functionalities in organic molecules. Following the recent discovery that cytochrome P450 enzymes can catalyze the cyclization of arylsulfonyl azide compounds via an intramolecular C(sp(3))H amination reaction, we have explored here the CH amination reactivity of other hemoproteins. Various heme-containing proteins, and in particular myoglobin and horseradish peroxidase, were found to be capable of catalyzing this transformation. Based on this finding, a series of engineered and artificial myoglobin variants containing active site mutations and non-native Mn- and Co-protoporphyrin IX cofactors, respectively, were prepared to investigate the effect of these structural changes on the catalytic activity and selectivity of these catalysts. Our studies showed that metallo-substituted myoglobins constitute viable CH amination catalysts, revealing a distinctive reactivity trend as compared to synthetic metalloporphyrin counterparts. On the other hand, amino acid substitutions at the level of the heme pocket were found to be beneficial toward improving the stereo- and enantioselectivity of these Mb-catalyzed reactions. Mechanistic studies involving kinetic isotope effect experiments indicate that CH bond cleavage is implicated in the rate-limiting step of myoglobin-catalyzed amination of arylsulfonyl azides. Altogether, these studies indicate that myoglobin constitutes a promising scaffold for the design and development of CH amination catalysts.
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