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

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

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

http://www.wikidata.org/entity/Q37351308

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Active Site Threonine Facilitates Proton Transfer during Dioxygen Activation at the Diiron Center of Toluene/ o -Xylene Monooxygenase Hydroxylase Tracking a defined route for O2 migration in a dioxygen-activating diiron enzyme Revisiting the mechanism of dioxygen activation in soluble methane monooxygenase from M. capsulatus (Bath): evidence for a multi-step, proton-dependent reaction pathway.A flexible glutamine regulates the catalytic activity of toluene o-xylene monooxygenase.Component interactions and electron transfer in toluene/o-xylene monooxygenase.Multiple roles of component proteins in bacterial multicomponent monooxygenases: phenol hydroxylase and toluene/o-xylene monooxygenase from Pseudomonas sp. OX1.Insights into the different dioxygen activation pathways of methane and toluene monooxygenase hydroxylases Mechanistic studies of reactions of peroxodiiron(III) intermediates in T201 variants of toluene/o-xylene monooxygenase hydroxylase Protonation of a peroxodiiron(III) complex and conversion to a diiron(III/IV) intermediate: implications for proton-assisted O-O bond cleavage in nonheme diiron enzymes.Single Turnover Reveals Oxygenated Intermediates in Toluene/o-Xylene Monooxygenase in the Presence of the Native Redox Partners Modeling the syn disposition of nitrogen donors in non-heme diiron enzymes. Synthesis, characterization, and hydrogen peroxide reactivity of diiron(III) complexes with the syn N-donor ligand H2BPG2DEV.Cyanobacterial aldehyde deformylase oxygenation of aldehydes yields n-1 aldehydes and alcohols in addition to alkanes.Structure/function correlations over binuclear non-heme iron active sites Single turnover kinetics of tryptophan hydroxylase: evidence for a new intermediate in the reaction of the aromatic amino acid hydroxylases.The prediction of Fe Mössbauer parameters by the density functional theory: a benchmark study.Unprecedented (μ-1,1-Peroxo)diferric Structure for the Ambiphilic Orange Peroxo Intermediate of the Nonheme N-Oxygenase CmlI.Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.Peroxide Activation for Electrophilic Reactivity by the Binuclear Non-heme Iron Enzyme AurF.Unexpected weak magnetic exchange coupling between haem and non-haem iron in the catalytic site of nitric oxide reductase (NorBC) from Paracoccus denitrificans1.

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

http://www.wikidata.org/entity/Q37351308

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on May 2009

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Characterization of a peroxodiiron

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Characterization of a peroxodi ...... ylase from Pseudomonas sp. OX1

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type

label

Characterization of a peroxodiiron

@nl

Characterization of a peroxodi ...... ylase from Pseudomonas sp. OX1

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prefLabel

Characterization of a peroxodiiron

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Characterization of a peroxodi ...... ylase from Pseudomonas sp. OX1

@en

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Journal of the American Chemical Society

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Characterization of a peroxodi ...... ylase from Pseudomonas sp. OX1

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Boi Hanh Huynh

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Rachel K Behan

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Sunil G Naik

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Woon Ju Song

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P2860

Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane

Structure and function of the Escherichia coli ribonucleotide reductase protein R2

Dioxygen Activation at Non-Heme Diiron Centers: Oxidation of a Proximal Residue in the I100W Variant of Toluene/ o -Xylene Monooxygenase Hydroxylase †

Structural consequences of effector protein complex formation in a diiron hydroxylase

Structures of deoxy and oxy hemerythrin at 2.0 A resolution

Expression and purification of the recombinant subunits of toluene/o-xylene monooxygenase and reconstitution of the active complex.

Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins A list of abbreviations can be found in Section 7.

Radical initiation in the class I ribonucleotide reductase: long-range proton-coupled electron transfer?

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

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

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6074-6075

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scholarly article

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10.1021/JA9011782

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17

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131

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Stephen J. Lippard

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2009-05-01T00:00:00Z

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24264644

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19354250

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2745944

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