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View article: Effects of ligand topology and iron coordination number on the electronic structure of FeIII-μ-oxo-CrIII complexes supported by tetramethylcyclam
Effects of ligand topology and iron coordination number on the electronic structure of FeIII-μ-oxo-CrIII complexes supported by tetramethylcyclam Open
57Fe Mössbauer, electron paramagnetic resonance, and 57Fe nuclear resonance vibrational spectroscopies are applied to characterize three different FeIII-O-CrIII complexes derived from the tetramethylcyclam (TMC, 1,4,8,11-tetramethyl-1,4,8,…
View article: Nature of the Reactive Biferric Peroxy Intermediate P′ in the Arylamine Oxygenases and Related Binuclear Fe Enzymes
Nature of the Reactive Biferric Peroxy Intermediate P′ in the Arylamine Oxygenases and Related Binuclear Fe Enzymes Open
Binuclear nonheme iron enzymes activate O2 to perform a wide range of chemical transformations. The process of O2 activation typically involves a biferric peroxy-level intermediate P. It has been previously found that this intermediate und…
View article: Experimental electronic structures of the Fe <sup>IV</sup> =O bond in S=1 heme vs. nonheme sites: Effect of the porphyrin ligand
Experimental electronic structures of the Fe <sup>IV</sup> =O bond in S=1 heme vs. nonheme sites: Effect of the porphyrin ligand Open
High-valent Fe IV =O species are common intermediates in biological and artificial catalysts. Heme and nonheme S=1 Fe IV =O sites have been synthesized and studied for decades but little quantitative experimental comparison of their electr…
View article: A 5,000-fold increase in the HAT reactivity of a nonheme Fe <sup>IV</sup> =O complex simply by replacing two pyridines of the pentadentate N4Py ligand with pyrazoles
A 5,000-fold increase in the HAT reactivity of a nonheme Fe <sup>IV</sup> =O complex simply by replacing two pyridines of the pentadentate N4Py ligand with pyrazoles Open
A pentadentate [N5] ligand (N2Py2Pz) based on the classic N4Py ( N,N -bis(2-pyridylmethyl)- N -bis(2-pyridyl)methylamine) framework has been synthesized by replacing the two pyridylmethyl arms with corresponding ( N -methyl)pyrazolylmethyl…
View article: Mimicking sMMOH chemistry: trapping the Sc <sup>3+</sup> -bound nonheme Fe <sup>III</sup> –O–O–Fe <sup>III</sup> adduct prior to its conversion into an Fe <sup>IV</sup> <sub>2</sub> (μ-O) <sub>2</sub> core
Mimicking sMMOH chemistry: trapping the Sc <sup>3+</sup> -bound nonheme Fe <sup>III</sup> –O–O–Fe <sup>III</sup> adduct prior to its conversion into an Fe <sup>IV</sup> <sub>2</sub> (μ-O) <sub>2</sub> core Open
The data in this paper represent the first documented evidence for Lewis-acid adduct formation to a 1,2-peroxodiferric species derived from the reaction of a diiron( ii ) complex with O 2 en route to its conversion into an Fe IV 2 (μ-O) 2 …
View article: Experimental Definition of the <i>S</i> = 1 π vs <i>S</i> = 2 σ Reactivity and <i>S</i> = 2 Character in the Ground State of an <i>S</i> = 1 Fe<sup>IV</sup>O Complex
Experimental Definition of the <i>S</i> = 1 π vs <i>S</i> = 2 σ Reactivity and <i>S</i> = 2 Character in the Ground State of an <i>S</i> = 1 Fe<sup>IV</sup>O Complex Open
Iron(IV)-oxo intermediates found in iron enzymes and artificial catalysts are competent for H atom abstraction in catalytic cycles. For S = 2 intermediates, both axial and equatorial approaches are well-established. The mechanism for S = 1…
View article: A tale of two topological isomers: Uptuning [Fe <sup>IV</sup> (O)(Me <sub>4</sub> cyclam)] <sup>2+</sup> for olefin epoxidation
A tale of two topological isomers: Uptuning [Fe <sup>IV</sup> (O)(Me <sub>4</sub> cyclam)] <sup>2+</sup> for olefin epoxidation Open
TMC- anti and TMC- syn, the two topological isomers of [Fe IV (O)(TMC)(CH 3 CN)] 2+ (TMC = 1,4,8,11-tetramethyl-1,4,8,11-tetraazacyclotetradecane, or Me 4 cyclam), differ in the orientations of their Fe IV =O units relative to the four met…
View article: NMR and Mössbauer Studies Reveal a Temperature-Dependent Switch from <i>S</i> = 1 to 2 in a Nonheme Oxoiron(IV) Complex with Faster C–H Bond Cleavage Rates
NMR and Mössbauer Studies Reveal a Temperature-Dependent Switch from <i>S</i> = 1 to 2 in a Nonheme Oxoiron(IV) Complex with Faster C–H Bond Cleavage Rates Open
S = 2 FeIV═O centers generated in the active sites of nonheme iron oxygenases cleave substrate C-H bonds at rates significantly faster than most known synthetic FeIV═O complexes. Unlike the majority of the latter, which are S = 1 complexes…
View article: Class Ib Ribonucleotide Reductases: Activation of a Peroxido-Mn<sup>II</sup>Mn<sup>III</sup> to Generate a Reactive Oxo-Mn<sup>III</sup>Mn<sup>IV</sup> Oxidant
Class Ib Ribonucleotide Reductases: Activation of a Peroxido-Mn<sup>II</sup>Mn<sup>III</sup> to Generate a Reactive Oxo-Mn<sup>III</sup>Mn<sup>IV</sup> Oxidant Open
In the postulated catalytic cycle of class Ib Mn2 ribonucleotide reductases (RNRs), a MnII2 core is suggested to react with superoxide (O2·-) to generate peroxido-MnIIMnIII and oxo-MnIIIMnIV entities prior to proton-coupled electron transf…
View article: 10 <sup>6</sup> -fold faster C–H bond hydroxylation by a Co <sup>III,IV</sup> <sub>2</sub> (µ-O) <sub>2</sub> complex [via a Co <sup>III</sup> <sub>2</sub> (µ-O)(µ-OH) intermediate] versus its Fe <sup>III</sup> Fe <sup>IV</sup> analog
10 <sup>6</sup> -fold faster C–H bond hydroxylation by a Co <sup>III,IV</sup> <sub>2</sub> (µ-O) <sub>2</sub> complex [via a Co <sup>III</sup> <sub>2</sub> (µ-O)(µ-OH) intermediate] versus its Fe <sup>III</sup> Fe <sup>IV</sup> analog Open
The hydroxylation of C–H bonds can be carried out by the high-valent Co III,IV 2 (µ-O) 2 complex 2a supported by the tetradentate tris(2-pyridylmethyl)amine ligand via a Co III 2 (µ-O)(µ-OH) intermediate ( 3a ). Complex 3a can be independe…
View article: Formation of a Reactive [Mn(III)−O−Ce(IV)] Species and its Facile Equilibrium with Related Mn(IV)(OX) (X = Sc or H) Complexes
Formation of a Reactive [Mn(III)−O−Ce(IV)] Species and its Facile Equilibrium with Related Mn(IV)(OX) (X = Sc or H) Complexes Open
Lewis acid‐bound high valent Mn‐oxo species are of great importance due to their relevance to photosystem II. Here, we report the synthesis of a unique [(BnTPEN)Mn(III)−O−Ce(IV)(NO 3 ) 4 ] + adduct ( 2 ) by the reaction of (BnTPEN)Mn(II) (…
View article: CCDC 2111625: Experimental Crystal Structure Determination
CCDC 2111625: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: CCDC 2111624: Experimental Crystal Structure Determination
CCDC 2111624: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: CCDC 2111623: Experimental Crystal Structure Determination
CCDC 2111623: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: CSD 1420966: Experimental Crystal Structure Determination
CSD 1420966: Experimental Crystal Structure Determination Open
An entry from the Inorganic Crystal Structure Database, the world’s repository for inorganic crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely availabl…
View article: Nonheme Diiron Oxygenase Mimic That Generates a Diferric–Peroxo Intermediate Capable of Catalytic Olefin Epoxidation and Alkane Hydroxylation Including Cyclohexane
Nonheme Diiron Oxygenase Mimic That Generates a Diferric–Peroxo Intermediate Capable of Catalytic Olefin Epoxidation and Alkane Hydroxylation Including Cyclohexane Open
Herein are described substrate oxidations with H2O2 catalyzed by [FeII(IndH)(CH3CN)3](ClO4)2 [IndH = 1,3-bis(2'-pyridylimino)isoindoline], involving a spectroscopically characterized (μ-oxo)(μ-1,2-peroxo)diiron(III) intermediate (2) that i…
View article: Explorations of the nonheme high-valent iron-oxo landscape: crystal structure of a synthetic complex with an [FeIV2(μ-O)<sub>2</sub>] diamond core relevant to the chemistry of sMMOH
Explorations of the nonheme high-valent iron-oxo landscape: crystal structure of a synthetic complex with an [FeIV2(μ-O)<sub>2</sub>] diamond core relevant to the chemistry of sMMOH Open
A synthetic mimic for the putative FeIV2O 2 diamond core of sMMOH-Q.
View article: CCDC 2034427: Experimental Crystal Structure Determination
CCDC 2034427: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: Unmasking Steps in Intramolecular Aromatic Hydroxylation by a Synthetic Nonheme Oxoiron(IV) Complex
Unmasking Steps in Intramolecular Aromatic Hydroxylation by a Synthetic Nonheme Oxoiron(IV) Complex Open
In this study, a methyl group on the classic tetramethylcyclam (TMC) ligand framework is replaced with a benzylic group to form the metastable [Fe IV (O syn )(Bn3MC)] 2+ ( 2 ‐syn; Bn3MC=1‐benzyl‐4,8,11‐trimethyl‐1,4,8,11‐tetraazacyclotetra…
View article: Spontaneous Formation of an Fe/Mn Diamond Core: Models for the Fe/Mn Sites in Class 1c Ribonucleotide Reductases
Spontaneous Formation of an Fe/Mn Diamond Core: Models for the Fe/Mn Sites in Class 1c Ribonucleotide Reductases Open
A handful of oxygen-activating enzymes has recently been found to contain Fe/Mn active sites, like Class 1c ribonucleotide reductases and R2-like ligand-binding oxidase, which are closely related to their better characterized diiron cousin…
View article: Tuning the H‐Atom Transfer Reactivity of Iron(IV)‐Oxo Complexes as Probed by Infrared Photodissociation Spectroscopy
Tuning the H‐Atom Transfer Reactivity of Iron(IV)‐Oxo Complexes as Probed by Infrared Photodissociation Spectroscopy Open
Reactivities of non‐heme iron(IV)‐oxo complexes are mostly controlled by the ligands. Complexes with tetradentate ligands such as [(TPA)FeO] 2+ (TPA=tris(2‐pyridylmethyl)amine) belong to the most reactive ones. Here, we show a fine‐tuning …
View article: Tuning the H‐Atom Transfer Reactivity of Iron(IV)‐Oxo Complexes as Probed by Infrared Photodissociation Spectroscopy
Tuning the H‐Atom Transfer Reactivity of Iron(IV)‐Oxo Complexes as Probed by Infrared Photodissociation Spectroscopy Open
Reactivities of non‐heme iron(IV)‐oxo complexes are mostly controlled by the ligands. Complexes with tetradentate ligands such as [(TPA)FeO] 2+ (TPA=tris(2‐pyridylmethyl)amine) belong to the most reactive ones. Here, we show a fine‐tuning …
View article: Ce<sup>IV</sup>‐ and HClO<sub>4</sub>‐Promoted Assembly of an Fe<sub>2</sub><sup>IV</sup>(μ‐O)<sub>2</sub> Diamond Core from its Monomeric Fe<sup>IV</sup>=O Precursor at Room Temperature
Ce<sup>IV</sup>‐ and HClO<sub>4</sub>‐Promoted Assembly of an Fe<sub>2</sub><sup>IV</sup>(μ‐O)<sub>2</sub> Diamond Core from its Monomeric Fe<sup>IV</sup>=O Precursor at Room Temperature Open
Diiron(IV)‐oxo species are proposed to effect the cleavage of strong C−H bonds by nonheme diiron enzymes such as soluble methane monooxygenase (sMMO) and fatty acid desaturases. However, synthetic mimics of such diiron(IV) oxidants are rar…
View article: Sc<sup>3+</sup>-Promoted O–O Bond Cleavage of a (μ-1,2-Peroxo)diiron(III) Species Formed from an Iron(II) Precursor and O<sub>2</sub> to Generate a Complex with an Fe<sup>IV</sup><sub>2</sub>(μ-O)<sub>2</sub> Core
Sc<sup>3+</sup>-Promoted O–O Bond Cleavage of a (μ-1,2-Peroxo)diiron(III) Species Formed from an Iron(II) Precursor and O<sub>2</sub> to Generate a Complex with an Fe<sup>IV</sup><sub>2</sub>(μ-O)<sub>2</sub> Core Open
Soluble methane monooxygenase (sMMO) carries out methane oxidation at 4 °C and under ambient pressure in a catalytic cycle involving the formation of a peroxodiiron(III) intermediate (P) from the oxygenation of the diiron(II) enzyme and it…