ArticleChemical communications (Cambridge, England)2020
Oxidation of an indole substrate by porphyrin iron(iii) superoxide: relevance to indoleamine and tryptophan 2,3-dioxygenases.
Article in Chemical communications (Cambridge, England), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- Janus Reactivity of a Mononuclear Non-Heme Iron(III)-Peroxo Complex Toward Indole Oxidation.Angewandte Chemie (International ed. in English) · 2026Article
- Evidence for the Formation of an Iron(III)-Indolenylperoxo Intermediate During Indole Dioxygenation: Similarities with Heme Dioxygenases.Inorganic chemistry · 2026Article
- Manganese-Substituted Polyoxometalates as Functional Mimics of Indole Dioxygenase Enzymes.Inorganic chemistry · 2026Article
- Nonheme iron catalyst mimics heme-dependent haloperoxidase for efficient bromination and oxidation.Science advances · 2024Article
- Secondary Sphere Lewis Acid Activated Heme Superoxo Adducts Mimic Crucial Non-Covalent Interactions in IDO/TDO Heme Dioxygenases.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- An Iron(III) Superoxide Corrole from Iron(II) and Dioxygen.Angewandte Chemie (International ed. in English) · 2022Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Reaction of FeIII(O2˙-)(TPP) with 2,3-dimethylindole at -40 °C gives the ring-opened, dioxygenated N-(2-acetyl-phenyl)-acetamide product. The reaction was monitored in situ by low-temperature UV-vis and 1H NMR spectroscopies. This work demonstrates that a discrete iron(iii)(superoxo) porphyrin is competent to carry out indole oxidation, as proposed for the tryptophan and indoleamine 2,3-dioxygenases.
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Registered trials
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