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

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

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

http://www.wikidata.org/entity/Q41280148

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Evolution of strategies to prepare synthetic mimics of carboxylate-bridged diiron protein active sites 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 Active Site Threonine Facilitates Proton Transfer during Dioxygen Activation at the Diiron Center of Toluene/ o -Xylene Monooxygenase Hydroxylase Structure and Mechanism of the Diiron Benzoyl-Coenzyme A Epoxidase BoxB Tracking a defined route for O2 migration in a dioxygen-activating diiron enzyme The catalase activity of diiron adenine deaminase Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases 2-Phenoxypyridyl dinucleating ligands for assembly of diiron(II) complexes: efficient reactivity with O(2) to form (mu-Oxo)diiron(III) units Carboxylate as the protonation site in (Peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins.A flexible glutamine regulates the catalytic activity of toluene o-xylene monooxygenase.Synthesis, Characterization, and Oxygenation Studies of Carboxylate-Bridged Diiron(II) Complexes with Aromatic Substrates Tethered to Pyridine Ligands and the Formation of a Unique Trinuclear Complex.Kinetic characterization of the soluble butane monooxygenase from Thauera butanivorans, formerly 'Pseudomonas butanovora'.Current challenges of modeling diiron enzyme active sites for dioxygen activation by biomimetic synthetic complexes Mössbauer, electron paramagnetic resonance, and density functional theory studies of synthetic S = 1/2 Fe(III)-O-Fe(IV)═O complexes. Superexchange-mediated spin transition at the Fe(IV)═O site.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 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.Substrate-triggered activation of a synthetic [Fe2(μ-O)2] diamond core for C-H bond cleavage.Single Turnover Reveals Oxygenated Intermediates in Toluene/o-Xylene Monooxygenase in the Presence of the Native Redox Partners Aging-associated enzyme human clock-1: substrate-mediated reduction of the diiron center for 5-demethoxyubiquinone hydroxylation.Hydrogen-bonding effects on the reactivity of [X-Fe(III)-O-Fe(IV)═O] (X = OH, F) complexes toward C-H bond cleavage.Characterization of a peroxodiiron(III) intermediate in the T201S variant of toluene/o-xylene monooxygenase hydroxylase from Pseudomonas sp. OX1 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.Substrate-triggered addition of dioxygen to the diferrous cofactor of aldehyde-deformylating oxygenase to form a diferric-peroxide intermediate.A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus Metal use in ribonucleotide reductase R2, di-iron, di-manganese and heterodinuclear--an intricate bioinorganic workaround to use different metals for the same reaction.Catalytic oxygen activation versus autoxidation for industrial applications: a physicochemical approach.Structure/function correlations over binuclear non-heme iron active sites Divergent mechanisms of iron-containing enzymes for hydrocarbon biosynthesis.X-ray absorption spectroscopic characterization of the diferric-peroxo intermediate of human deoxyhypusine hydroxylase in the presence of its substrate eIF5a Molecular determinants of the regioselectivity of toluene/o-xylene monooxygenase from Pseudomonas sp. strain OX1 An unusual peroxo intermediate of the arylamine oxygenase of the chloramphenicol biosynthetic pathway.New mechanistic insights into intramolecular aromatic ligand hydroxylation and benzyl alcohol oxidation initiated by the well-defined (μ-peroxo)diiron(iii) complex.In-crystal reaction cycle of a toluene-bound diiron hydroxylase.New mechanistic insight into intramolecular arene hydroxylation initiated by (μ-1,2-peroxo)diiron(III) complexes with dinucleating ligands.Unprecedented (μ-1,1-Peroxo)diferric Structure for the Ambiphilic Orange Peroxo Intermediate of the Nonheme N-Oxygenase CmlI.

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P2860

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

http://www.wikidata.org/entity/Q41280148

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2007 nî lūn-bûn

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2007年の論文

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年學術文章

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2007年學術文章

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2007年學術文章

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name

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

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type

label

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

@en

prefLabel

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

@en

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P1433

Journal of the American Chemical Society

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

@en

P2093

Boi Hanh Huynh

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Danilo O Ortillo

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Jessica K Lee

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Ricardo García-Serres

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Sunil G Naik

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Immunochemical detection of oxidized proteins.

X-ray crystal structures of reduced rubrerythrin and its azide adduct: a structure-based mechanism for a non-heme diiron peroxidase

X-ray Structure of a Hydroxylase−Regulatory Protein Complex from a Hydrocarbon-Oxidizing Multicomponent Monooxygenase, Pseudomonas sp. OX1 Phenol Hydroxylase † , ‡

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

Crystal structure of delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins

Evidence for C-H cleavage by an iron-superoxide complex in the glycol cleavage reaction catalyzed by myo-inositol oxygenase

Generation and characterization of [(P)M-(X)-Co(TMPA)]n+ assemblies; P = Porphyrinate, M = FeIII and CoIII, X = O2-, OH-, O2(2-), and TMPA = tris(2-pyridylmethyl)amine.

Intermediates in the oxygenation of a nonheme diiron(II) complex, including the first evidence for a bound superoxo species

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.

High-valent iron(IV)-oxo complexes of heme and non-heme ligands in oxygenation reactions.

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10.1021/JA076121H

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129

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Stephen J. Lippard

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2007-10-30T00:00:00Z

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