Evidence map›Paper›PMID 17967027›Full record

ArticleJournal of the American Chemical Society2007

Characterization of the arene-oxidizing intermediate in ToMOH as a diiron(III) species.

Leslie J Murray, Sunil G Naik, Danilo O Ortillo, Ricardo García-Serres, Jessica K Lee, Boi Hanh Huynh, Stephen J Lippard

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structure and assembly of the diiron cofactor in the heme-oxygenase-like domain of theProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Article
  6. A Peroxodiiron(III/III) Intermediate Mediating BothJournal of the American Chemical Society · 2020
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Divergent mechanisms of iron-containing enzymes for hydrocarbon biosynthesis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017
    Review
  12. 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
  13. X-ray absorption spectroscopic characterization of the diferric-peroxo intermediate of human deoxyhypusine hydroxylase in the presence of its substrate eIF5a.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  18. Article
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Leslie J MurrayDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Sunil G Naik
Danilo O Ortillo
Ricardo García-Serres
Jessica K Lee
Boi Hanh Huynh
Stephen J Lippard
Massachusetts Institute of Technology · USEmory University · 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
LIGAND-BRIDGED POLYNUCLEAR METAL COMPLEXES &PROTEINSR37GM032134 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LIPPARD, STEPHEN J · 1988 to 1997
–
NIGMS NIH HHS GM32134NIGMS NIH HHS GM 47295NIGMS NIH HHS R01 GM032134NIGMS NIH HHS R01 GM047295
6 · The paper itself

Abstract

We report the generation and characterization of a diiron(III) intermediate formed during reaction with dioxygen of the reduced hydroxylase component of toluene/o-xylene monooxygenase from Pseudomonas sp. OX1. The decay rate of this species is accelerated upon mixing with phenol, a substrate for this system. Under steady-state conditions, hydrogen peroxide was generated in the absence of substrate. The oxidized hydroxylase also decomposed hydrogen peroxide to liberate dioxygen in the absence of reducing equivalents. This activity suggests that dioxygen activation may be reversible. The linear free energy relationship determined from hydroxylation of para-substituted phenols under steady-state turnover has a negative slope. A value of rho < 0 is consistent with electrophilic attack by the oxidizing intermediate on the aromatic substrates. The results from these steady and pre-steady-state experiments provide compelling evidence that the diiron(III) intermediate is the active oxidant in the toluene/o-xylene monooxygenase system and is a peroxodiiron(III) transient, despite differences between its optical and Mössbauer spectroscopic parameters and those of other peroxodiiron(III) centers.

Indexed as

CatalaseFerric CompoundsHydrocarbons, AromaticHydrogen PeroxideHydroxylationKineticsMixed Function OxygenasesOxidation-ReductionOxygenOxygenasesPhenolsPseudomonasSpectroscopy, MossbauerCatalaseFerric CompoundsHydrocarbons, AromaticHydrogen PeroxideMixed Function OxygenasesOxygenOxygenasesPhenolstoluene 2-xylene monooxygenase

Identifiers

PMID17967027
PMCPMC2494525
OpenAlexW2053009800

What OpenQuestion holds

Textmetadata
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.