A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus - Wikidata - awgldk - TriplyDB

A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus

A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus

http://www.wikidata.org/entity/Q37410598

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Evolution of strategies to prepare synthetic mimics of carboxylate-bridged diiron protein active sites Structure and mechanism of ORF36, an amino sugar oxidizing enzyme in everninomicin biosynthesis .Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases Conversion of Aldehyde to Alkane by a Peroxoiron(III) Complex: A Functional Model for the Cyanobacterial Aldehyde-Deformylating Oxygenase Four-electron oxidation of p-hydroxylaminobenzoate to p-nitrobenzoate by a peroxodiferric complex in AurF from Streptomyces thioluteus.Evidence that the fosfomycin-producing epoxidase, HppE, is a non-heme-iron peroxidase Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase.Active-site structure of a β-hydroxylase in antibiotic biosynthesis Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase.Cyanobacterial alkane biosynthesis further expands the catalytic repertoire of the ferritin-like 'di-iron-carboxylate' proteins.Mechanistic studies of reactions of peroxodiiron(III) intermediates in T201 variants of toluene/o-xylene monooxygenase hydroxylase Characterization of a synthetic peroxodiiron(III) protein model complex by nuclear resonance vibrational spectroscopy.O(2)-evolving chlorite dismutase as a tool for studying O(2)-utilizing enzymes.Structural, EPR, and Mössbauer characterization of (μ-alkoxo)(μ-carboxylato)diiron(II,III) model complexes for the active sites of mixed-valent diiron enzymes.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.Systematic Perturbations of Binuclear Non-heme Iron Sites: Structure and Dioxygen Reactivity of de Novo Due Ferri Proteins.CmlI is an N-oxygenase in the biosynthesis of chloramphenicol Substrate-triggered addition of dioxygen to the diferrous cofactor of aldehyde-deformylating oxygenase to form a diferric-peroxide intermediate.Novel Approaches for the Accumulation of Oxygenated Intermediates to Multi-Millimolar Concentrations.Circular dichroism, magnetic circular dichroism, and variable temperature variable field magnetic circular dichroism studies of biferrous and mixed-valent myo-inositol oxygenase: insights into substrate activation of O2 reactivity.Cyanobacterial aldehyde deformylase oxygenation of aldehydes yields n-1 aldehydes and alcohols in addition to alkanes.Naturally-occurring nitro compounds.Time-Resolved Investigations of Heterobimetallic Cofactor Assembly in R2lox Reveal Distinct Mn/Fe Intermediates.Structure/function correlations over binuclear non-heme iron active sites Divergent mechanisms of iron-containing enzymes for hydrocarbon biosynthesis.Heteroatom-Heteroatom Bond Formation in Natural Product Biosynthesis.Alteration of the oxygen-dependent reactivity of de novo Due Ferri proteins.Molecular-Level Insight into the Differential Oxidase and Oxygenase Reactivities of de Novo Due Ferri Proteins.Crystal structure of CmlI, the arylamine oxygenase from the chloramphenicol biosynthetic pathway.X-ray absorption spectroscopic characterization of the diferric-peroxo intermediate of human deoxyhypusine hydroxylase in the presence of its substrate eIF5a Mechanism for Six-Electron Aryl-N-Oxygenation by the Non-Heme Diiron Enzyme CmlI.An unusual peroxo intermediate of the arylamine oxygenase of the chloramphenicol biosynthetic pathway.CmlI N-Oxygenase Catalyzes the Final Three Steps in Chloramphenicol Biosynthesis without Dissociation of Intermediates.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.Diiron monooxygenases in natural product biosynthesis.

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P2860

A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus

http://www.wikidata.org/entity/Q37410598

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on September 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

A long-lived, substrate-hydrox ...... , from Streptomyces thioluteus

@en

A long-lived, substrate-hydrox ...... from Streptomyces thioluteus.

@nl

type

label

A long-lived, substrate-hydrox ...... , from Streptomyces thioluteus

@en

A long-lived, substrate-hydrox ...... from Streptomyces thioluteus.

@nl

prefLabel

A long-lived, substrate-hydrox ...... , from Streptomyces thioluteus

@en

A long-lived, substrate-hydrox ...... from Streptomyces thioluteus.

@nl

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Journal of the American Chemical Society

P1476

A long-lived, substrate-hydrox ...... , from Streptomyces thioluteus

@en

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Eric W Barr

http://www.w3.org/2001/XMLSchema#string

J Martin Bollinger

http://www.w3.org/2001/XMLSchema#string

Ning Li

http://www.w3.org/2001/XMLSchema#string

Victoria Korneeva Korboukh

http://www.w3.org/2001/XMLSchema#string

P2860

Structure and action of the N-oxygenase AurF from Streptomyces thioluteus

In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis

AurF from Streptomyces thioluteus and a possible new family of manganese/iron oxygenases.

Intermediates in dioxygen activation by methane monooxygenase: a QM/MM study.

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

Use of a chemical trigger for electron transfer to characterize a precursor to cluster X in assembly of the iron-radical cofactor of Escherichia coli ribonucleotide reductase.

Nature of the peroxo intermediate of the W48F/D84E ribonucleotide reductase variant: implications for O2 activation by binuclear non-heme iron enzymes.

Sequential enzymatic oxidation of aminoarenes to nitroarenes via hydroxylamines.

Evidence for two ferryl species in chloroperoxidase compound II.

A new class of arylamine oxygenases: evidence that p-aminobenzoate N-oxygenase (AurF) is a di-iron enzyme and further mechanistic studies.

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13608-13609

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scholarly article

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10.1021/JA9064969

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38

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131

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2009-09-01T00:00:00Z

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26791027

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19731912

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2772654

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