Optically pure sulfoxides are noteworthy compounds that find wide applications in various industrial fields. Here, we report a methionine sulfoxide reductase B (MsrB) homologue that exhibits high enantioselectivity and broad substrate scope for the kinetic resolution of racemic () sulfoxides. This MsrB homologue, named MsrB, was identified from sp. 103DPR2 and showed good activity together with enantioselectivity towards a series of aromatic, heteroaromatic, alkyl and thioalkyl sulfoxides. Chiral sulfoxides in the configuration were prepared in approximately 50% yield and 92-99% enantiomeric excess through kinetic resolution at an initial substrate concentration of up to 90 mM (11.2 g L). This study presents an efficient route for the enzymatic preparation of ()-sulfoxides through kinetic resolution.
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http://dx.doi.org/10.1039/d3ob00402c | DOI Listing |
J Am Chem Soc
December 2024
Department of Chemistry and the Hong Kong Branch of Chinese National Engineering Research Centre for Tissue Restoration & Reconstruction, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR 999077, China.
Catalytic enantioselective substitution of the readily available racemic α-halo carbonyl compounds by nitrogen nucleophiles represents one of the most convenient and direct approaches to access enantioenriched α-amino carbonyl compounds. Distinct from the two available strategies involving radicals and enolate ions, herein we have developed a new protocol featuring an electronically opposite way to weaken/cleave the carbon-halogen bond. A suitable chiral anion-based catalyst enables effective asymmetric control over the key positively charged intermediates.
View Article and Find Full Text PDFTalanta
December 2024
Marshall Laboratory of Biomedical Engineering, Shenzhen Key Laboratory for Nano-Biosensing Technology, Department of Biomedical Engineering, Medical School, Shenzhen University, Shenzhen, Guangdong, 518060, PR China. Electronic address:
Colorimetric enzyme-linked immunosorbent assays (CELISAs) have long been used for protein biomarker detection in diagnostics. Unfortunately, as confined by the monochromatic nature of detection signals and the limited catalytic activity of enzymes, CELISAs suffer from poor visual resolution and low sensitivity, hindering their effectiveness for early diagnostics in resource-limited settings. Herein, we report an ultrasensitive, high-visual-resolution CELISA (named PE-TSA-AuAg Cage-CELISA) that combines kinetically controlled growth of Ag in AuAg nanocages with poly-enzyme-boosted tyramide signal amplification (PE-TSA), enabling visual semiquantitative detection of protein biomarkers at attomolar levels with the naked eye.
View Article and Find Full Text PDFACS Catal
December 2024
Stratingh Institute for Chemistry, University of Groningen, Groningen 9747 AG, The Netherlands.
Genetically encoded noncanonical amino acids can introduce new-to-nature activation modes into enzymes. While these amino acids can act as catalysts on their own due to their inherent chemical properties, interactions with adjacent residues in an enzyme, such as those present in natural catalytic dyads or triads, unlock a higher potential for designer enzymes. We incorporated a boron-containing amino acid into the protein scaffold RamR to create an active enzyme for the kinetic resolution of α-hydroxythioesters.
View Article and Find Full Text PDFJ Am Chem Soc
December 2024
Department of Chemical and Biological Engineering, Institute of Chemical Processes, Seoul National University, Seoul 08826, Republic of Korea.
Electrochemical liquid-cell transmission electron microscopy (e-LCTEM) offers great potential for investigating the structural dynamics of nanomaterials during electrochemical reactions. However, challenges arise from the difficulty in achieving the optimal electrolyte thickness, leading to inconsistent electrochemical responses and limited spatial resolution. In this study, we present advanced e-LCTEM techniques tailored for tracking Pt/C degradation under electrochemical polarization at short intervals with high spatial resolution.
View Article and Find Full Text PDFACS Nano
December 2024
Department of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, United States.
Two or more protein ligands may compete against each other to interact transiently with a protein receptor. While this is a ubiquitous phenomenon in cell signaling, existing technologies cannot identify its kinetic complexity because specific subpopulations of binding events of different ligands are hidden in the averaging process in an ensemble. In addition, the limited time resolution of prevailing methods makes detecting and discriminating binding events among diverse interacting partners challenging.
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