Evidence map›Paper›PMID 21574560›Full record

ArticleJournal of the American Chemical Society2011

An ENDOR and HYSCORE investigation of a reaction intermediate in IspG (GcpE) catalysis.

Weixue Wang, Ke Wang, Jikun Li, Saritha Nellutla, Tatyana I Smirnova, Eric Oldfield

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. An [FeJournal of the American Chemical Society · 2020
    Article
  5. A Synthetic Model of Enzymatic [FeJournal of the American Chemical Society · 2019
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Advanced electron paramagnetic resonance on the catalytic iron-sulfur cluster bound to the CCG domain of heterodisulfide reductase and succinate: quinone reductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013
    Article
  11. Isoprenoid biosynthesis: ferraoxetane or allyl anion mechanism for IspH catalysis?Angewandte Chemie (International ed. in English) · 2013
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Structure, function and inhibition of the two- and three-domain 4Fe-4S IspG proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

6 authors.

Weixue WangCenter for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, 607 South Mathews Avenue, Urbana, Illinois 61801, USA.
Ke Wang
Jikun Li
Saritha Nellutla
Tatyana I Smirnova
Eric Oldfield

Funding

Structure, Function and Inhibition of [4Fe-4S] ProteinsR01GM065307 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI OLDFIELD, ERIC · 2002 to 2017
$5.4M
Protein Structure/Function by NMR, Crystallography and Computational ChemistryR01AI074233 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI OLDFIELD, ERIC · 2008 to 2012
$1.8M
Time-domain/ELDOR EPR SpectrometerS10RR023614 · NCRR · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI SMIRNOV, ALEX I. · 2009 to 2009
$500k
Multifrequency Pulsed Electron Paramagnetic Resonance Spectrometer For BiomedicalS10RR025438 · NCRR · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI DIKANOV, SERGEI A · 2009 to 2009
$397k
NCRR NIH HHS S10 RR023614NCRR NIH HHS S10RR023614NCRR NIH HHS S10 RR025438NCRR NIH HHS S10RR025438NIAID NIH HHS AI074233NIAID NIH HHS R01 AI074233NIGMS NIH HHS GM065307NIGMS NIH HHS R01 GM065307
6 · The paper itself

Abstract

IspG is a 4Fe-4S protein that carries out an essential reduction step in isoprenoid biosynthesis. Using electron-nuclear double resonance (ENDOR) and hyperfine sublevel correlation (HYSCORE) spectroscopies on labeled samples, we have specifically assigned the hyperfine interactions in a reaction intermediate. These results help clarify the nature of the reaction intermediate, supporting a direct interaction between the unique fourth Fe in the cluster and C2 and O3 of the ligand.

Indexed as

Alkyl and Aryl TransferasesCatalysisElectron Spin Resonance SpectroscopyEnzymesModels, MolecularMolecular StructureAlkyl and Aryl TransferasesEnzymeshydroxymethylbutenyl 4-diphosphate synthase

Identifiers

PMID21574560
PMCPMC3116442

What OpenQuestion holds

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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.