ArticleBiochemistry2020
Kinetic and Spectroscopic Characterization of the Catalytic Ternary Complex of Tryptophan 2,3-Dioxygenase.
Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Compensatory pathways in tryptophan metabolism and immune regulation following IDO inhibition.Molecular biology reports · 2026Review
- Evidence for the Formation of an Iron(III)-Indolenylperoxo Intermediate During Indole Dioxygenation: Similarities with Heme Dioxygenases.Inorganic chemistry · 2026Article
- Provision of a Redox Donor to Oxy-Ferrous PrnB Is Required for Pyrrolnitrin Synthesis.Biochemistry · 2025Article
- 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
- Hydroxytryptophan biosynthesis by a family of heme-dependent enzymes in bacteria.Nature chemical biology · 2023Article
- Capturing aBiochemistry · 2023Article
- 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
- A novel catalytic heme cofactor in SfmD with a single thioether bond and aChemical science · 2021Article
- Nature's Machinery, Repurposed: Expanding the Repertoire of Iron-Dependent Oxygenases.ACS catalysis · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The first step of the kynurenine pathway for l-tryptophan (l-Trp) degradation is catalyzed by heme-dependent dioxygenases, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase. In this work, we employed stopped-flow optical absorption spectroscopy to study the kinetic behavior of the Michaelis complex of
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Registered trials
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