ArticleThe Journal of biological chemistry2009
Ligand and substrate migration in human indoleamine 2,3-dioxygenase.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- One Key and Multiple Locks: Substrate Binding in Structures of Tryptophan Dioxygenases and Hydroxylases.ChemMedChem · 2021Review
- Conformational Plasticity in Human Heme-Based Dioxygenases.Journal of the American Chemical Society · 2021Article
- Advances in indoleamine 2,3-dioxygenase 1 medicinal chemistry.MedChemComm · 2017Review
- 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
- Different Mechanisms of Catalytic Complex Formation in Two L-Tryptophan Processing Dioxygenases.Frontiers in molecular biosciences · 2017Review
- The mechanism of substrate inhibition in human indoleamine 2,3-dioxygenase.Journal of the American Chemical Society · 2012Article
- Ferryl derivatives of human indoleamine 2,3-dioxygenase.The Journal of biological chemistry · 2011Article
- Ligand migration in human indoleamine-2,3 dioxygenase.IUBMB life · 2011Article
- Spectroscopic studies of ligand and substrate binding to human indoleamine 2,3-dioxygenase.Biochemistry · 2010Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Human indoleamine 2,3-dioxygenase (hIDO), a monomeric heme enzyme, catalyzes the oxidative degradation of L-Trp and other indoleamine derivatives. Using Fourier transform infrared and optical absorption spectroscopy, we have investigated the interplay between ferrous hIDO, the ligand analog CO, and the physiological substrate L-Trp. These data provide the long sought evidence for two distinct L-Trp binding sites. Upon photodissociation from the heme iron at T > 200 K, CO escapes into the solvent. Concomitantly, L-Trp exits the active site and, depending on the l-Trp concentration, migrates to a secondary binding site or into the solvent. Although L-Trp is spectroscopically silent at this site, it is still noticeable due to its pronounced effect on the CO association kinetics, which are significantly slower than those of L-Trp-free hIDO. L-Trp returns to its initial site only after CO has rebound to the heme iron.
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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.