ArticleJournal of the American Chemical Society2018
Stepwise O-Atom Transfer in Heme-Based Tryptophan Dioxygenase: Role of Substrate Ammonium in Epoxide Ring Opening.
Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- 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
- Single-atom substitution redirects KatG reactivity from cofactor biogenesis to stereoselective sulfoxidation.Nature communications · 2026Article
- Monooxygenase Activity of Indoleamine 2,3-Dioxygenase.Journal of the American Chemical Society · 2026Article
- Substrate Analogs Implicate a Free Radical Pathway in Tyrosine Hydroxylase Catalysis.ACS catalysis · 2025Article
- Deciphering Tryptophan Oxygenation: Key Modulators of 2-Oxindole Formation in MarE.Angewandte Chemie (International ed. in English) · 2025Article
- Study on the Therapeutic Effect and Mechanism of Gu Pi Sheng Ji Hua Zhuo Jie Du Decoction in Inducing Remission of Crohn's Disease.International journal of general medicine · 2025Article
- Heme-based dioxygenases: Structure, function and dynamics.Journal of inorganic biochemistry · 2024Review
- Hydroxytryptophan biosynthesis by a family of heme-dependent enzymes in bacteria.Nature chemical biology · 2023Article
- Structural insights into the half-of-sites reactivity in homodimeric and homotetrameric metalloenzymes.Current opinion in chemical biology · 2023Review
- Indoleamine 2,3-Dioxygenase as a Therapeutic Target for Alzheimer's Disease and Geriatric Depression.Brain sciences · 2023Review
- Tryptophan Can Promote Oxygen Reduction to Water in a Biosynthetic Model of Heme Copper Oxidases.Biochemistry · 2023Article
- Oxygen versus Sulfur Coordination in Cobalt Superoxo Complexes: Spectroscopic Properties, OInorganic chemistry · 2023Article
- Combined spectroscopic and structural approaches to explore the mechanism of histidine-ligated heme-dependent aromatic oxygenases.Methods in enzymology · 2023Article
- A new regime of heme-dependent aromatic oxygenase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- A novel catalytic heme cofactor in SfmD with a single thioether bond and aChemical science · 2021Article
- Developing C2-Aroyl Indoles as Novel Inhibitors of IDO1 and Understanding Their Mechanism of InhibitionFrontiers in chemistry · 2021Article
- Kinetic and Spectroscopic Characterization of the Catalytic Ternary Complex of Tryptophan 2,3-Dioxygenase.Biochemistry · 2020Article
- Oxidation of an indole substrate by porphyrin iron(iii) superoxide: relevance to indoleamine and tryptophan 2,3-dioxygenases.Chemical communications (Cambridge, England) · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Heme-based tryptophan dioxygenases are established immunosuppressive metalloproteins with significant biomedical interest. Here, we synthesized two mechanistic probes to specifically test if the α-amino group of the substrate directly participates in a critical step of the O atom transfer during catalysis in human tryptophan 2,3-dioxygenase (TDO). Substitution of the nitrogen atom of the substrate to a carbon (probe 1) or oxygen (probe 2) slowed the catalytic step following the first O atom transfer such that transferring the second O atom becomes less likely to occur, although the dioxygenated products were observed with both probes. A monooxygenated product was also produced from probe 2 in a significant quantity. Analysis of this new product by HPLC coupled UV-vis spectroscopy, high-resolution mass spectrometry,
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.