ArticleProceedings of the National Academy of Sciences of the United States of America2012
Indole peroxygenase activity of indoleamine 2,3-dioxygenase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 47 citations in OpenAlex.
- Engineered indoleamine 2,3-dioxygenase variant: Oxidative activation of prodrug indole-3-acetic acid against cancer cells for targeted therapy.Molecular therapy. Oncology · 2026Article
- Less is more: miniaturized heme enzymes with broad reactivity.Chemical science · 2026Review
- Monooxygenase Activity of Indoleamine 2,3-Dioxygenase.Journal of the American Chemical Society · 2026Article
- Oxidative Rearrangement of Indoles Enabled by Promiscuous Cryptic Halogenation with Vanadium-Dependent Haloperoxidases.ACS catalysis · 2026Article
- Provision of a Redox Donor to Oxy-Ferrous PrnB Is Required for Pyrrolnitrin Synthesis.Biochemistry · 2025Article
- Production of indigo by recombinant bacteria.Bioresources and bioprocessing · 2023Review
- Function of reactive oxygen species in myeloid-derived suppressor cells.Frontiers in immunology · 2023Review
- Indoleamine 2,3-dioxygenase 1 (IDO1): an up-to-date overview of an eclectic immunoregulatory enzyme.The FEBS journal · 2022Review
- A new regime of heme-dependent aromatic oxygenase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- IDO1 scavenges reactive oxygen species in myeloid-derived suppressor cells to prevent graft-versus-host disease.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A novel catalytic heme cofactor in SfmD with a single thioether bond and aChemical science · 2021Article
- An overview of microbial indigo-forming enzymes.Applied microbiology and biotechnology · 2020Review
- Flavin Conjugated Polydopamine Nanoparticles Displaying Light-Driven Monooxygenase Activity.Frontiers in chemistry · 2019Article
- A short history of heme dioxygenases: rise, fall and rise again.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Peroxygenase and oxidase activities of dehaloperoxidase-hemoglobin from Amphitrite ornata.Journal of the American Chemical Society · 2014Article
- Tryptophan-catabolizing enzymes - party of three.Frontiers in immunology · 2014Review
- Human indoleamine 2,3-dioxygenase is a catalyst of physiological heme peroxidase reactions: implications for the inhibition of dioxygenase activity by hydrogen peroxide.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The heme enzyme indoleamine 2,3-dioxygenase (IDO) was found to catalyze the oxidation of indole by H(2)O(2), with generation of 2- and 3-oxoindole as the major products. This reaction occurred in the absence of O(2) and reducing agents and was not inhibited by superoxide dismutase or hydroxyl radical scavengers, although it was strongly inhibited by L-Trp. The stoichiometry of the reaction indicated a one-to-one correspondence for the consumption of indole and H(2)O(2). The (18)O-labeling experiments indicated that the oxygen incorporated into the monooxygenated products was derived almost exclusively from H(2)(18)O(2), suggesting that electron transfer was coupled to the transfer of oxygen from a ferryl intermediate of IDO. These results demonstrate that IDO oxidizes indole by means of a previously unrecognized peroxygenase activity. We conclude that IDO inserts oxygen into indole in a reaction that is mechanistically analogous to the "peroxide shunt" pathway of cytochrome P450.
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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.