ArticleBiochemistry2015
Rapid kinetics of dehalogenation promoted by iodotyrosine deiodinase from human thyroid.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Article
- Misregulation of bromotyrosine compromises fertility in maleProceedings of the National Academy of Sciences of the United States of America · 2024Article
- 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
- Light-driven Oxidative Demethylation Reaction Catalyzed by a Rieske-type Non-heme Iron Enzyme Stc2.ACS catalysis · 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
- Evolutionary aspects of the Viridiplantae nitroreductases.Journal, genetic engineering & biotechnology · 2020Article
- Redox control of iodotyrosine deiodinase.Protein science : a publication of the Protein Society · 2019Article
- Oxidative dehalogenation and denitration by a flavin-dependent monooxygenase is controlled by substrate deprotonation.Chemical science · 2018Article
- The importance of a halotyrosine dehalogenase forThe Journal of biological chemistry · 2018Article
- The distribution and mechanism of iodotyrosine deiodinase defied expectations.Archives of biochemistry and biophysics · 2017Review
- A molecular view of the normal human thyroid structure and function reconstructed from its reference transcriptome map.BMC genomics · 2017Article
- Kinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA.The Journal of biological chemistry · 2017Article
- Active Site Binding Is Not Sufficient for Reductive Deiodination by Iodotyrosine Deiodinase.Biochemistry · 2017Article
- Functional analysis of iodotyrosine deiodinase from drosophila melanogaster.Protein science : a publication of the Protein Society · 2016Article
- The metabolism and de-bromination of bromotyrosine in vivo.Free radical biology & medicine · 2016Article
- Single Amino Acid Switch between a Flavin-Dependent Dehalogenase and Nitroreductase.Journal of the American Chemical Society · 2015Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Reductive dehalogenation such as that catalyzed by iodotyrosine deiodinase (IYD) is highly unusual in aerobic organisms but necessary for iodide salvage from iodotyrosine generated during thyroxine biosynthesis. Equally unusual is the dependence of this process on flavin. Rapid kinetics have now been used to define the basic processes involved in IYD catalysis. Time-dependent quenching of flavin fluorescence was used to monitor halotyrosine association to IYD. The substrates chloro-, bromo-, and iodotyrosine bound with similar rate constants (kon) ranging from 1.3 × 10(6) to 1.9 × 10(6) M(-1) s(-1). Only the inert substrate analogue fluorotyrosine exhibited a significantly (5-fold) slower kon (0.3 × 10(6) M(-1) s(-1)). All data fit a standard two-state model and indicated that no intermediate complex accumulated during closure of the active site lid induced by substrate. Subsequent halide elimination does not appear to limit reactions of bromo- and iodotyrosine since both fully oxidized the reduced enzyme with nearly equivalent second-order rate constants (7.3 × 10(3) and 8.6 × 10(3) M(-1) s(-1), respectively) despite the differing strength of their carbon-halogen bonds. In contrast to these substrates, chlorotyrosine reacted with the reduced enzyme approximately 20-fold more slowly and revealed a spectral intermediate that formed at approximately the same rate as the bromo- and iodotyrosine reactions.
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