ArticleAngewandte Chemie (International ed. in English)2025
Artificial Gold Enzymes Using a Genetically Encoded Thiophenol-Based Noble-Metal-Binding Ligand.
Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Artificial metalloenzymes in complex biological environments.Nature chemical biology · 2026Review
- Bioorthogonal Gold-Catalyzed Hydrothiolation Leading to Amide Bond Cleavage of Ethynylated Biarylbutanamide Precursors.Journal of the American Chemical Society · 2026Article
- Exploring PadR Proteins for Artificial Enzyme Design.Chembiochem : a European journal of chemical biology · 2026Article
- Engineering Fluoroacetate Dehalogenase by Growth-Based Selections on Non-Natural Organofluorides.Angewandte Chemie (International ed. in English) · 2026Article
- Engineering LmrR protein for L-proline-based asymmetric aldol biocatalysis.Nature communications · 2026Article
- Article
- A Genetically Encoded Homocysteine Precursor to Probe Protein Active Sites and to Addict Escherichia coli to a Noncanonical Amino Acid Directly Involved in Catalysis.Angewandte Chemie (International ed. in English) · 2025Article
- Orthogonal Site-Specific Dual Bioconjugation of Aryl and Alkyl Thiols.Journal of the American Chemical Society · 2025Article
- Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025Review
- Artificial Gold Enzymes Using a Genetically Encoded Thiophenol-Based Noble-Metal-Binding Ligand.Angewandte Chemie (International ed. in English) · 2025Article
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6 authors.
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Abstract
Incorporating noble metals in artificial metalloenzymes (ArMs) is challenging due to the lack of suitable soft coordinating ligands among natural amino acids. We present a new class of ArMs featuring a genetically encoded noble-metal-binding site based on a non-canonical thiophenol-based amino acid, 4-mercaptophenylalanine (pSHF), incorporated in the transcriptional regulator LmrR through stop codon suppression. We demonstrate that pSHF is an excellent ligand for noble metals in their low oxidation states. The corresponding gold(I) enzyme was characterised by mass spectrometry, UV/Vis spectroscopy and X-ray crystallography and successfully catalysed hydroamination reactions of 2-ethynyl anilines with turnover numbers over 50. Interestingly, two equivalents of gold(I) per protein dimer proved to be required for activity. Up to 98 % regioselectivity in the hydroamination of an ethynylphenylurea substrate was observed, yielding the corresponding phenyl-dihydroquinazolinone product, consistent with a π-activation mechanism by single gold centres. The ArM was optimized by site saturation mutagenesis using an on-bead screening protocol. This resulted in a single mutant that showed higher activity for one class of substrates. This work brings the power of noble-metal catalysis into the realm of enzyme engineering and establishes thiophenols as alternative ligands for noble metals, providing new opportunities in coordination chemistry and catalysis.
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