ArticleThe Journal of biological chemistry2015
A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 49 citations in OpenAlex.
- pK Values of the Cofactor Tune the Redox Regime of Flavoenzymes.Life (Basel, Switzerland) · 2026Article
- Article
- Polar Interactions between Substrate and Flavin Control Iodotyrosine Deiodinase Function.Biochemistry · 2024Article
- Article
- Misregulation of bromotyrosine compromises fertility in maleProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.Natural product reports · 2023Review
- 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
- 1IUCrData · 2023Article
- Derivatives of Natural Organocatalytic Cofactors and Artificial Organocatalytic Cofactors as Catalysts in Enzymes.Chembiochem : a European journal of chemical biology · 2022Review
- Sequence Conservation Does Not Always Signify a Functional Imperative as Observed in the Nitroreductase Superfamily.Biochemistry · 2022Article
- Structures and function of a tailoring oxidase in complex with a nonribosomal peptide synthetase module.Nature communications · 2022Article
- Comprehensive analysis of the amino acid metabolism-related gene signature for prognosis, tumor immune microenvironment, and candidate drugs in hepatocellular carcinoma.Frontiers in immunology · 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
- Cryo-EM: A new dawn in thyroid biology.Molecular and cellular endocrinology · 2021Review
- Evolutionary aspects of the Viridiplantae nitroreductases.Journal, genetic engineering & biotechnology · 2020Article
- Spectroscopic evidence for direct flavin-flavin contact in a bifurcating electron transfer flavoprotein.The Journal of biological chemistry · 2020Article
- Emerging strategies for expanding the toolbox of enzymes in biocatalysis.Current opinion in chemical biology · 2020Review
- Biocatalytic hydrogen atom transfer: an invigorating approach to free-radical reactions.Current opinion in chemical biology · 2019Review
- Redox control of iodotyrosine deiodinase.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Reductive dehalogenation is not typical of aerobic organisms but plays a significant role in iodide homeostasis and thyroid activity. The flavoprotein iodotyrosine deiodinase (IYD) is responsible for iodide salvage by reductive deiodination of the iodotyrosine derivatives formed as byproducts of thyroid hormone biosynthesis. Heterologous expression of the human enzyme lacking its N-terminal membrane anchor has allowed for physical and biochemical studies to identify the role of substrate in controlling the active site geometry and flavin chemistry. Crystal structures of human IYD and its complex with 3-iodo-l-tyrosine illustrate the ability of the substrate to provide multiple interactions with the isoalloxazine system of FMN that are usually provided by protein side chains. Ligand binding acts to template the active site geometry and significantly stabilize the one-electron-reduced semiquinone form of FMN. The neutral form of this semiquinone is observed during reductive titration of IYD in the presence of the substrate analog 3-fluoro-l-tyrosine. In the absence of an active site ligand, only the oxidized and two-electron-reduced forms of FMN are detected. The pH dependence of IYD binding and turnover also supports the importance of direct coordination between substrate and FMN for productive catalysis.
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