ArticleThe Journal of biological chemistry2011
Ferryl derivatives of human indoleamine 2,3-dioxygenase.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation.Nature communications · 2021Article
- Kinetic and Spectroscopic Characterization of the Catalytic Ternary Complex of Tryptophan 2,3-Dioxygenase.Biochemistry · 2020Article
- Inhibition Mechanisms of Human Indoleamine 2,3 Dioxygenase 1.Journal of the American Chemical Society · 2018Article
- Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.Chemical reviews · 2018Review
- Structural insights into substrate and inhibitor binding sites in human indoleamine 2,3-dioxygenase 1.Nature communications · 2017Article
- Different Mechanisms of Catalytic Complex Formation in Two L-Tryptophan Processing Dioxygenases.Frontiers in molecular biosciences · 2017Review
- Structural Study of a Flexible Active Site Loop in Human Indoleamine 2,3-Dioxygenase and Its Functional Implications.Biochemistry · 2016Article
- Peroxygenase and oxidase activities of dehaloperoxidase-hemoglobin from Amphitrite ornata.Journal of the American Chemical Society · 2014Article
- 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
- Indole peroxygenase activity of indoleamine 2,3-dioxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- NADH oxidase activity of indoleamine 2,3-dioxygenase.The Journal of biological chemistry · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The critical role of the ferryl intermediate in catalyzing the oxygen chemistry of monooxygenases, oxidases, or peroxidases has been known for decades. In contrast, its involvement in heme-based dioxygenases, such as human indoleamine 2,3-dioxygenase (hIDO), was not recognized until recently. In this study, H(2)O(2) was used as a surrogate to generate the ferryl intermediate of hIDO. Spectroscopic data demonstrate that the ferryl species is capable of oxidizing azinobis(3-ethylbenzothiazoline-6-sulfonic acid) but not L-Trp. Kinetic studies reveal that the conversion of the ferric enzyme to the ferryl intermediate facilitates the L-Trp binding rate by >400-fold; conversely, L-Trp binding to the enzyme retards the peroxide reaction rate by ∼9-fold, because of the significant elevation of the entropic barrier. The unfavorable entropic factor for the peroxide reaction highlights the scenario that the structure of hIDO is not optimized for utilizing H(2)O(2) as a co-substrate for oxidizing L-Trp. Titration studies show that the ferryl intermediate possesses two substrate-binding sites with a K(d) of 0.3 and 440 μM and that the electronic properties of the ferryl moiety are sensitive to the occupancy of the two substrate-binding sites. The implications of the data are discussed in the context of the structural and functional relationships of the enzyme.
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