ArticleNature2016
Accessing non-natural reactivity by irradiating nicotinamide-dependent enzymes with light.
Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.
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Who cites it
121 citing papers in PubMed, 418 citations in OpenAlex.
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- Niacin in your bread, NAD in your lab.Nature chemistry · 2026Article
- Harnessing Photoenzymatic Systems for Intermolecular C-H Fluorination.Angewandte Chemie (International ed. in English) · 2026Article
- Asymmetric Hydrogen Atom Transfer.ACS catalysis · 2026Review
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Designing and Engineering Enzymes for New-to-Nature Photobiocatalysis.Methods in molecular biology (Clifton, N.J.) · 2026Review
- A pyridoxal radical carboligase and imine reductase photobiocatalytic cascade for stereoselective synthesis of unnatural prolines.Nature chemistry · 2026Article
- Photoenzymatic catalysis enables enantioselective radical dearomative spirocyclization.Nature communications · 2025Article
- Biocatalytic kinetic resolution for efficient and enantioselective synthesis of δ-haloalcohols and tetrahydrofurans.Communications chemistry · 2025Article
- Catalyst-free photoinduced dehalogenation and functionalization of alkyl halides using Lewis bases.RSC advances · 2025Article
- Aromatic Coupling Reactions Catalyzed by "ene"-Reductase under Visible Light Irradiation.ACS omega · 2025Article
61 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymes are ideal for use in asymmetric catalysis by the chemical industry, because their chemical compositions can be tailored to a specific substrate and selectivity pattern while providing efficiencies and selectivities that surpass those of classical synthetic methods. However, enzymes are limited to reactions that are found in nature and, as such, facilitate fewer types of transformation than do other forms of catalysis. Thus, a longstanding challenge in the field of biologically mediated catalysis has been to develop enzymes with new catalytic functions. Here we describe a method for achieving catalytic promiscuity that uses the photoexcited state of nicotinamide co-factors (molecules that assist enzyme-mediated catalysis). Under irradiation with visible light, the nicotinamide-dependent enzyme known as ketoreductase can be transformed from a carbonyl reductase into an initiator of radical species and a chiral source of hydrogen atoms. We demonstrate this new reactivity through a highly enantioselective radical dehalogenation of lactones-a challenging transformation for small-molecule catalysts. Mechanistic experiments support the theory that a radical species acts as an intermediate in this reaction, with NADH and NADPH (the reduced forms of nicotinamide adenine nucleotide and nicotinamide adenine dinucleotide phosphate, respectively) serving as both a photoreductant and the source of hydrogen atoms. To our knowledge, this method represents the first example of photo-induced enzyme promiscuity, and highlights the potential for accessing new reactivity from existing enzymes simply by using the excited states of common biological co-factors. This represents a departure from existing light-driven biocatalytic techniques, which are typically explored in the context of co-factor regeneration.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.