Evidence map›Paper›PMID 26744902›Full record

ArticleBiochemistry2016

Formation of Hexacoordinate Mn(III) in Bacillus subtilis Oxalate Decarboxylase Requires Catalytic Turnover.

Wen Zhu, Jarett Wilcoxen, R David Britt, Nigel G J Richards

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2016. 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
6.2field-weighted citation impact, top 5% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Oxalate decarboxylase uses electron hole hopping for catalysis.The Journal of biological chemistry · 2021
    Article
  6. Article
  7. Mn(III) species formed by the multi-copper oxidase MnxG investigated by electron paramagnetic resonance spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Article
  8. Article
  9. Oxygen activation by mononuclear Mn, Co, and Ni centers in biology and synthetic complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017
    Review
  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

4 authors at 2 institutions in 1 country.

Wen ZhuDepartment of Chemistry & Chemical Biology, Indiana University Purdue University Indianapolis , Indianapolis, Indiana 46202, United States.
Jarett WilcoxenDepartment of Chemistry, University of California , Davis, California 95616, United States.
R David BrittDepartment of Chemistry, University of California , Davis, California 95616, United States.
Nigel G J RichardsDepartment of Chemistry & Chemical Biology, Indiana University Purdue University Indianapolis , Indianapolis, Indiana 46202, United States.
Indiana University – Purdue University Indianapolis · USUniversity of California, Davis · US

Funding

Biochemical Studies of Oxalate DecarboxylaseR01DK061666 · NIDDK · UNIVERSITY OF FLORIDA · PI RICHARDS, NIGEL GORDON · 2003 to 2013
$1.9M
Mechanisms of Radical SAM Enzymes Probed by EPR SpectroscopyR01GM104543 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI BRITT, R DAVID · 2014 to 2017
$1.2M
Biochemical Studies of Oxalate DecarboxylaseR56DK061666 · NIDDK · UNIVERSITY OF FLORIDA · PI RICHARDS, NIGEL GORDON · 2008 to 2008
$205k
NIDDK NIH HHS DK-061666NIDDK NIH HHS R01 DK061666NIDDK NIH HHS R56 DK061666NIGMS NIH HHS GM-104543NIGMS NIH HHS R01 GM104543
6 · The paper itself

Abstract

Oxalate decarboxylase (OxDC) catalyzes the disproportionation of oxalic acid monoanion into CO2 and formate. The enzyme has long been hypothesized to utilize dioxygen to form mononuclear Mn(III) or Mn(IV) in the catalytic site during turnover. Recombinant OxDC, however, contains only tightly bound Mn(II), and direct spectroscopic detection of the metal in higher oxidation states under optimal catalytic conditions (pH 4.2) has not yet been reported. Using parallel mode electron paramagnetic resonance spectroscopy, we now show that substantial amounts of Mn(III) are indeed formed in OxDC, but only in the presence of oxalate and dioxygen under acidic conditions. These observations provide the first direct support for proposals in which Mn(III) removes an electron from the substrate to yield a radical intermediate in which the barrier to C-C bond cleavage is significantly decreased. Thus, OxDC joins a small list of enzymes capable of stabilizing and controlling the reactivity of the powerful oxidizing species Mn(III).

Indexed as

Bacillus subtilisBacterial ProteinsBiocatalysisCarboxy-LyasesCoordination ComplexesElectron Spin Resonance SpectroscopyHydrogen-Ion ConcentrationManganeseOxalatesOxidation-ReductionOxygenRecombinant ProteinsBacterial ProteinsCarboxy-LyasesCoordination ComplexesManganeseoxalate decarboxylaseOxalatesOxygenRecombinant Proteins

Identifiers

PMID26744902
PMCPMC8183094
OpenAlexW2223264101

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.