Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Journal of the American Chemical Society - 6 May 2009

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

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Epoxy Compounds
Share to Ferric Compounds

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Variation

Share to Mutation

Share to Oxygenases

Share to Pseudomonas

Source

Open in PubMed Open full text

Identifiers

PMID: 19354250
DOI: 10.1021/ja9011782
PMCID: PMC2745944

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of a peroxodiiron(III) intermediate in the T201S variant of toluene/o-xylene monooxygenase hydroxylase from Pseudomonas sp. OX1.PMID 19354250Read ↗

Dioxygen activation at non-heme diiron centers: characterization of intermediates in a mutant form of toluene/o-xylene monooxygenase hydroxylase.Semantic proximity Read ↗

Dioxygen activation at non-heme diiron centers: oxidation of a proximal residue in the I100W variant of toluene/o-xylene monooxygenase hydroxylase.Semantic proximity Read ↗

Crystal structure of the toluene/o-xylene monooxygenase hydroxylase from Pseudomonas stutzeri OX1. Insight into the substrate specificity, substrate channeling, and active site tuning of multicomponent monooxygenases.Semantic proximity Read ↗

Tuning the specificity of the recombinant multicomponent toluene o-xylene monooxygenase from Pseudomonas sp. strain OX1 for the biosynthesis of tyrosol from 2-phenylethanol.Semantic proximity Read ↗

Alpha-subunit positions methionine 180 and glutamate 214 of Pseudomonas stutzeri OX1 toluene-o-xylene monooxygenase influence catalysis.Semantic proximity Read ↗

Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.Semantic proximity Read ↗

Protein engineering of toluene-o-xylene monooxygenase from Pseudomonas stutzeri OX1 for synthesizing 4-methylresorcinol, methylhydroquinone, and pyrogallol.Semantic proximity Read ↗

Amino acids located in the outer-sphere of the trinuclear copper center in a multicopper oxidase, CueO as the putative electron donor in the four-electron reduction of dioxygen.Semantic proximity Read ↗

Mutation of glutamic acid 103 of toluene o-xylene monooxygenase as a means to control the catabolic efficiency of a recombinant upper pathway for degradation of methylated aromatic compounds.Semantic proximity Read ↗

Peroxygenases en route to becoming dream catalysts. What are the opportunities and challenges?Semantic proximity Read ↗

Effect of distal His mutation on the peroxynitrite reactivity of Leishmania major peroxidase.Semantic proximity Read ↗

Regulation of methane monooxygenase catalysis based on size exclusion and quantum tunneling.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.