ArticleProtein science : a publication of the Protein Society2019
Redox control of iodotyrosine deiodinase.
Article in Protein science : a publication of the Protein Society, 2019. 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, 17 citations in OpenAlex.
- Polar Interactions between Substrate and Flavin Control Iodotyrosine Deiodinase Function.Biochemistry · 2024Article
- Article
- The 2'-hydroxy group of flavin mononucleotide influences the catalytic function and promiscuity of the flavoprotein iodotyrosine dehalogenase.RSC chemical biology · 2023Article
- Substrate Electronics Dominate the Rate of Reductive Dehalogenation Promoted by the Flavin-Dependent Iodotyrosine Deiodinase.Biochemistry · 2023Article
- Sequence Conservation Does Not Always Signify a Functional Imperative as Observed in the Nitroreductase Superfamily.Biochemistry · 2022Article
- Identification of Signature Genes in the PD-1 Relative Gastric Cancer Using a Combined Analysis of Gene Expression and Methylation Data.Journal of oncology · 2022Article
- The minimal structure for iodotyrosine deiodinase function is defined by an outlier protein from the thermophilic bacterium Thermotoga neapolitana.The Journal of biological chemistry · 2021Article
- Article
- Evolutionary aspects of the Viridiplantae nitroreductases.Journal, genetic engineering & biotechnology · 2020Article
- Structural basis for the hydrolytic dehalogenation of the fungicide chlorothalonil.The Journal of biological chemistry · 2020Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
The redox chemistry of flavoproteins is often gated by substrate and iodotyrosine deiodinase (IYD) has the additional ability to switch between reaction modes based on the substrate. Association of fluorotyrosine (F-Tyr), an inert substrate analog, stabilizes single electron transfer reactions of IYD that are not observed in the absence of this ligand. The co-crystal of F-Tyr and a T239A variant of human IYD have now been characterized to provide a structural basis for control of its flavin reactivity. Coordination of F-Tyr in the active site of this IYD closely mimics that of iodotyrosine and only minor perturbations are observed after replacement of an active site Thr with Ala. However, loss of the side chain hydroxyl group removes a key hydrogen bond from flavin and suppresses the formation of its semiquinone intermediate. Even substitution of Thr with Ser decreases the midpoint potential of human IYD between its oxidized and semiquinone forms of flavin by almost 80 mV. This decrease does not adversely affect the kinetics of reductive dehalogenation although an analogous Ala variant exhibits a 6.7-fold decrease in its k
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