Evidence map›Paper›PMID 26230193›Full record

ArticleBiochemistry2015

Biochemical and Spectroscopic Studies of Epoxyqueuosine Reductase: A Novel Iron-Sulfur Cluster- and Cobalamin-Containing Protein Involved in the Biosynthesis of Queuosine.

Zachary D Miles, William K Myers, William M Kincannon, R David Britt, Vahe Bandarian

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Metal retention and replacement in QueD2 protect queuosine-tRNA biosynthesis in metal-starvedProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Vitamin BCurrent opinion in chemical biology · 2017
    Review
  16. Review
  17. Article
  18. Elucidation of roles for vitamin BProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Article
  20. Review
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

5 authors at 2 institutions in 1 country.

Zachary D Miles†Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721, United States.
William K Myers‡Department of Chemistry, University of California-Davis, Davis, California 95616, United States.
William M Kincannon†Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721, United States.
R David Britt‡Department of Chemistry, University of California-Davis, Davis, California 95616, United States.
Vahe Bandarian†Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721, United States.
University of Arizona · USUniversity of California, Davis · US

Funding

CHEMISTRY-BIOLOGY INTERFACE TRAINING PROGRAMT32GM008804 · NIGMS · UNIVERSITY OF ARIZONA · PI MONTFORT, WILLIAM R. · 2003 to 2023
$3.9M
Biosynthesis of Deazapurine-Containing MetabolitesR01GM072623 · NIGMS · UNIVERSITY OF UTAH · PI BANDARIAN, VAHE · 2005 to 2017
$3.9M
Mechanisms of Radical SAM Enzymes Probed by EPR SpectroscopyR01GM104543 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI BRITT, R DAVID · 2014 to 2017
$1.2M
NIGMS NIH HHS R01 GM072623NIGMS NIH HHS R01 GM104543NIGMS NIH HHS R01GM72623NIGMS NIH HHS T32 GM008804
6 · The paper itself

Abstract

Queuosine is a hypermodified nucleoside present in the wobble position of tRNAs with a 5'-GUN-3' sequence in their anticodon (His, Asp, Asn, and Tyr). The 7-deazapurine core of the base is synthesized de novo in prokaryotes from guanosine 5'-triphosphate in a series of eight sequential enzymatic transformations, the final three occurring on tRNA. Epoxyqueuosine reductase (QueG) catalyzes the final step in the pathway, which entails the two-electron reduction of epoxyqueuosine to form queuosine. Biochemical analyses reveal that this enzyme requires cobalamin and two [4Fe-4S] clusters for catalysis. Spectroscopic studies show that the cobalamin appears to bind in a base-off conformation, whereby the dimethylbenzimidazole moiety of the cofactor is removed from the coordination sphere of the cobalt but not replaced by an imidazole side chain, which is a hallmark of many cobalamin-dependent enzymes. The bioinformatically identified residues are shown to have a role in modulating the primary coordination sphere of cobalamin. These studies provide the first demonstration of the cofactor requirements for QueG.

Indexed as

Bacillus subtilisBacterial ProteinsIron-Sulfur ProteinsNucleoside QOxidoreductasesVitamin B 12CatalysisBacterial ProteinsIron-Sulfur ProteinsNucleoside QOxidoreductasesVitamin B 12

Identifiers

PMID26230193
PMCPMC4753064
OpenAlexW1004589244

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.