Evidence map›Paper›PMID 30075052›Full record

ArticleAngewandte Chemie (International ed. in English)2018

Two-Color Valence-to-Core X-ray Emission Spectroscopy Tracks Cofactor Protonation State in a Class I Ribonucleotide Reductase.

Ryan J Martinie, Elizabeth J Blaesi, J Martin Bollinger, Carsten Krebs, Kenneth D Finkelstein, Christopher J Pollock

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The role of basicity in selective C-H bond activation by transition metal-oxidos.Dalton transactions (Cambridge, England : 2003) · 2023
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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.

Ryan J MartinieDepartment of Chemistry, The Pennsylvania State University, 318 Chemistry Building, University Park, PA, 16802, USA.ORCID 0000-0003-1257-2850
Elizabeth J BlaesiDepartment of Chemistry, The Pennsylvania State University, 318 Chemistry Building, University Park, PA, 16802, USA.ORCID 0000-0003-2601-8367
J Martin BollingerDepartment of Chemistry and Department of Biochemistry and Molecular Biology, The Pennsylvania State University, 318 Chemistry Building, University Park, PA, 16802, USA.ORCID 0000-0003-0751-8585
Carsten KrebsDepartment of Chemistry and Department of Biochemistry and Molecular Biology, The Pennsylvania State University, 318 Chemistry Building, University Park, PA, 16802, USA.ORCID 0000-0002-3302-7053
Kenneth D FinkelsteinCornell High Energy Synchrotron Source, Wilson Laboratory, Cornell University, Ithaca, NY, 14853, USA.ORCID 0000-0002-1851-2624
Christopher J PollockDepartment of Chemistry, The Pennsylvania State University, 318 Chemistry Building, University Park, PA, 16802, USA.ORCID 0000-0001-5736-513X

Funding

RIBONUCLEOTIDE REDUCTASE--IRON-RADICAL COFACTOR ASSEMBLYR01GM055365 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI BOLLINGER, JOSEPH M, GREEN, MICHAEL T. · 1997 to 2011
$3.2M
Mechanistic Determination of the Non-heme Iron Enzyme Hyoscyamine-6-hydroxylaseF32GM113389 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI POLLOCK, CHRISTOPHER · 2015 to 2017
$160k
Mechanisms of Radical Translocation in Class I Ribonucleotide ReductasesF32GM116353 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI BLAESI, ELIZABETH J · 2015 to 2017
$160k
NIGMS NIH HHS F32 GM113389NIGMS NIH HHS F32 GM116353NIGMS NIH HHS GM113389-01NIGMS NIH HHS GM116353-01NIGMS NIH HHS GM55365NIGMS NIH HHS R01 GM055365
6 · The paper itself

Abstract

Proton transfer reactions are of central importance to a wide variety of biochemical processes, though determining proton location and monitoring proton transfers in biological systems is often extremely challenging. Herein, we use two-color valence-to-core X-ray emission spectroscopy (VtC XES) to identify protonation events across three oxidation states of the O

Indexed as

Spectrometry, X-Ray EmissionBacterial ProteinsChlamydia trachomatisDensity Functional TheoryFerric CompoundsIonsIronManganeseProtonsRibonucleotide ReductasesBacterial ProteinsFerric CompoundsIonsIronManganeseProtonsRibonucleotide Reductasesbioinorganic chemistrymetalloenzymestwo-color techniquesvalence-to-coreX-ray emission spectroscopy

Identifiers

PMID30075052
PMCPMC6579043

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.