Evidence map›Paper›PMID 28774660›Full record

ReviewArchives of biochemistry and biophysics2017

The distribution and mechanism of iodotyrosine deiodinase defied expectations.

Zuodong Sun, Qi Su, Steven E Rokita

Abstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. ExaminingFrontiers in toxicology · 2026
    Article
  3. Article
  4. Biochemistry · 2024
    Article
  5. Misregulation of bromotyrosine compromises fertility in maleProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Redox control of iodotyrosine deiodinase.Protein science : a publication of the Protein Society · 2019
    Article
  14. The importance of a halotyrosine dehalogenase forThe Journal of biological chemistry · 2018
    Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Zuodong SunDepartment of Chemistry, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA.
Qi SuDepartment of Chemistry, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA.
Steven E RokitaDepartment of Chemistry, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA. Electronic address: rokita@jhu.edu.
Johns Hopkins University · US

Funding

Reductive Dehalogenation in Mammals by Iodotyrosine DeiodinaseR01DK084186 · NIDDK · UNIV OF MARYLAND, COLLEGE PARK · PI ROKITA, STEVEN E · 2009 to 2012
$1.3M
The Role of a Dehalogenase in Drosophila SpermatogenesisR21AI119540 · NIAID · JOHNS HOPKINS UNIVERSITY · PI ROKITA, STEVEN E · 2015 to 2016
$428k
NIAID NIH HHS R21 AI119540NIDDK NIH HHS R01 DK084186
6 · The paper itself

Abstract

Iodotyrosine deiodinase (IYD) is unusual for its reliance on flavin to promote reductive dehalogenation under aerobic conditions. As implied by the name, this enzyme was first discovered to catalyze iodide elimination from iodotyrosine for recycling iodide during synthesis of tetra- and triiodothyronine collectively known as thyroid hormone. However, IYD likely supports many more functions and has been shown to debrominate and dechlorinate bromo- and chlorotyrosines. A specificity for halotyrosines versus halophenols is well preserved from humans to bacteria. In all examples to date, the substrate zwitterion establishes polar contacts with both the protein and the isoalloxazine ring of flavin. Mechanistic data suggest dehalogenation is catalyzed by sequential one electron transfer steps from reduced flavin to substrate despite the initial expectations for a single two electron transfer mechanism. A purported flavin semiquinone intermediate is stabilized by hydrogen bonding between its N5 position and the side chain of a Thr. Mutation of this residue to Ala suppresses dehalogenation and enhances a nitroreductase activity that is reminiscent of other enzymes within the same structural superfamily.

Indexed as

AnimalsFlavin-Adenine DinucleotideHumansIodide PeroxidaseIodidesNitroreductasesTriiodothyronineFlavin-Adenine Dinucleotideflavin semiquinoneIodide PeroxidaseIodidesNitroreductasesTriiodothyronineDehalogenaseFlavinIodide salvageReductive dehalogenationThyroid

Identifiers

PMID28774660
PMCPMC5665059
OpenAlexW2740040187

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.