Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
The [Fe]/HO oxidation system has found wide applications in chemistry and biology. Halogenation with this [Fe]/HO oxidation protocol and halide (X) in the biological system is well established with the identification of heme-iron-dependent haloperoxidases. However, mimicking such halogenation process is rarely explored for practical use in organic synthesis. Here, we report the development of a nonheme iron catalyst that mimics the heme-iron-dependent haloperoxidases to catalyze the generation of HOBr from HO/Br with high efficiency. We discovered that a tridentate terpyridine (TPY) ligand designed for Fenton chemistry was optimal for FeBr to form a stable nonheme iron catalyst [Fe(TPY)Br], which catalyzed arene bromination, Hunsdiecker-type decarboxylative bromination, bromolactonization, and oxidation of sulfides and thiols. Mechanistic studies revealed that Fenton chemistry ([Fe]/HO) might operate to generate hydroxyl radical (HO), which oxidize bromide ion [Br] into reactive HOBr. This nonheme iron catalyst represents a biomimetic model for heme-iron-dependent haloperoxidases with potential applications in organic synthesis, drug discovery, and biology.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11616719 | PMC |
| http://dx.doi.org/10.1126/sciadv.adq0028 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Pirin does not bind to p65 or regulate NFκB-dependent gene expression but does modulate cellular quercetin levels.
Mol Pharmacol
August 2025
Department of Pharmacology and Toxicology, Michigan State University, East Lansing, Michigan; "Nicholas V. Perricone, M.D.," Division of Dermatology, Department of Medicine, Michigan State University, East Lansing, Michigan. Electronic address:
Pirin is a nonheme iron-binding protein with a variety of proposed functions, including serving as a coactivator of p65 NFκB and quercetinase activity. We report here, failure to confirm pirin's primary proposed mechanism, binding of Fe(III)-pirin and p65. Analytical size exclusion chromatography and fluorescence polarization studies did not detect an interaction.
View Article and Find Full Text PDFMechanistic Divergence in Sulfur-Ligated Iron(III)-Alkylperoxo Reactivity: Aldehyde Oxidation Prevails over Deformylation.
Angew Chem Int Ed Engl
September 2025
Department of Chemistry, Indian Institute of Technology, Guwahati, Assam, 781039, India.
Metalloenzymes activate molecular oxygen within their catalytic cycles to generate a reactive species capable of substrate transformation. In many iron-containing enzymes, it is a high-valent iron(IV)-oxo complex that is synthesized from an iron(III)-alkylperoxo intermediate, although direct observation and characterization of such species have remained elusive, leaving their mechanistic role uncertain. To address this gap in our understanding, we present here the synthesis, comprehensive characterization, and reactivity of a novel thioether-ligated iron(III)-alkylperoxo complex supported by the ligand 2-((2-(pyridin-2-yl)ethyl)thio)-N,N-bis(pyridin-2-ylmethyl)ethan-1-amine.
View Article and Find Full Text PDFStudies of Isonitrile Synthases Help Elucidate the Mechanism of Isonitrile Installation.
ACS Catal
July 2025
Department of Chemistry, North Carolina State University, Raleigh, NC 27695, USA.
Isonitrile functional group is abundant in natural products and associated with various biological properties. To date, two pathways are known for isonitrile group installation. One is catalyzed by mononuclear nonheme iron dependent isonitrilases in which the reaction mechanism involves consecutive desaturation and decarboxylation processes.
View Article and Find Full Text PDFRieske Oxygenases: Powerful Models for Understanding Nature's Orchestration of Electron Transfer and Oxidative Chemistry.
Biochemistry
August 2025
Department of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, Groningen 9713AV, Netherlands.
Rieske oxygenases (ROs) are a diverse family of nonheme iron enzymes that catalyze a wide array of oxidative transformations in both catabolic and biosynthetic pathways. Their catalytic repertoire spans dioxygenation, monooxygenation, oxidative - and -dealkylation, desaturation, sulfoxidation, C-C bond formation, -oxygenation, and C-N bond cleavage─reactions that are often challenging to achieve selectively through synthetic methods. These diverse functions highlight the increasing importance of ROs in natural product biosynthesis and establish them as promising candidates for biocatalytic applications.
View Article and Find Full Text PDFInvestigating the Synergistic Influence of Redox-Inactive Metal Ions at the Secondary Coordination Sphere of Non-Heme Iron Complexes on Oxygen Reduction Reaction.
Chem Asian J
August 2025
Department of Chemistry, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, 110016, India.
The secondary coordination sphere (SCS) around the substrate binding site of a catalyst, such as a proton relay, formation of a hydrogen bonding network, and electrostatic effects, plays a critical role in controlling the selectivity and rate of oxygen reduction reaction (ORR). Herein, we report the ORR study of a series of Fe complexes having a uniform primary coordination sphere and an unlike SCS. The Fe(III) complex, lacking any secondary coordination sphere (SCS) modifications, exhibited slow oxygen reduction reaction (ORR) kinetics in the presence of decamethylferrocene (Fc) and trifluoroacetic acid (TFAH) in oxygen-saturated acetonitrile.
View Article and Find Full Text PDF