Evidence map›Paper›PMID 19354250›Full record

ArticleJournal of the American Chemical Society2009

Characterization of a peroxodiiron(III) intermediate in the T201S variant of toluene/o-xylene monooxygenase hydroxylase from Pseudomonas sp. OX1.

Woon Ju Song, Rachel K Behan, Sunil G Naik, Boi Hanh Huynh, Stephen J Lippard

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. AccurateJournal of chemical theory and computation · 2021
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  6. Structure/function correlations over binuclear non-heme iron active sites.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Review
  7. Article
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  12. Tracking a defined route for O₂ migration in a dioxygen-activating diiron enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2011
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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.

Woon Ju SongDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Rachel K Behan
Sunil G Naik
Boi Hanh Huynh
Stephen J Lippard
Emory University · USMassachusetts Institute of Technology · US

Funding

NONHEME IRON AND THE BIOLOGICAL OXIDATION OF METHANER01GM032134 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LIPPARD, STEPHEN J. · 1985 to 2013
$6.9M
OXYGEN ACTIVATION BY NON HEME FE PROTEINSR01GM047295 · NIGMS · EMORY UNIVERSITY · PI HUYNH, BOI-HANH V. · 1992 to 2008
$1.7M
Evaluating Aspects of O2-Activation by Bacterial Multicomponent MonooxygenasesF32GM084564 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WOLLACOTT, RACHEL BEHAN · 2008 to 2010
$115k
LIGAND-BRIDGED POLYNUCLEAR METAL COMPLEXES &PROTEINSR37GM032134 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LIPPARD, STEPHEN J · 1988 to 1997
–
NIGMS NIH HHS 1 F32 GM084564-01NIGMS NIH HHS F32 GM084564NIGMS NIH HHS GM32134NIGMS NIH HHS GM 47295NIGMS NIH HHS R01 GM032134NIGMS NIH HHS R01 GM047295
6 · The paper itself

Abstract

We report the observation of a novel intermediate in the reaction of a reduced toluene/o-xylene monooxygenase hydroxylase (ToMOH(red)) T201S variant, in the presence of a regulatory protein (ToMOD), with dioxygen. This species is the first oxygenated intermediate with an optical band in any toluene monooxygenase. The UV-vis and Mossbauer spectroscopic properties of the intermediate allow us to assign it as a peroxodiiron(III) species, T201S(peroxo), similar to H(peroxo) in methane monooxygenase. Although T201S generates T201S(peroxo) in addition to optically transparent ToMOH(peroxo), previously observed in wild-type ToMOH, this conservative variant is catalytically active in steady-state catalysis and single-turnover experiments and displays the same regiospecificity for toluene and slightly different regiospecificity for o-xylene oxidation.

Indexed as

Epoxy CompoundsFerric CompoundsGenetic VariationMutationOxygenasesPseudomonasEpoxy CompoundsFerric CompoundsOxygenasestoluene 2-xylene monooxygenase

Identifiers

PMID19354250
PMCPMC2745944
OpenAlexW2172150348

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.