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Heme-Containing Oxygenases
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Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1006/abbi.1993.1231openalex-snapshot
Domains of Rat Heme Oxygenase-2: The Amino Terminus and Histidine 151 Are Required for Heme Oxidation
inferredcites →https://doi.org/10.1006/abbi.1995.1160openalex-snapshot
Demonstration That Histidine-25, But Not Histidine-132, Is the Axial Heme Ligand in Rat Heme Oxygenase-1
inferredcites →https://doi.org/10.1006/bbrc.1993.1197openalex-snapshot
Cytochrome P450-Butyl Peroxide Complex Detected by ESR
inferredcites →https://doi.org/10.1006/bbrc.1994.1852openalex-snapshot
Spectral Intermediate in the Reaction of Ferrous Cytochrome P450cam with Superoxide Anion
inferredcites →https://doi.org/10.1006/bbrc.1994.1868openalex-snapshot
Evidence for Compound I Formation in the Reaction of Cytochrome-P450cam with m-Chloroperbenzoic Acid
inferredcites →https://doi.org/10.1006/bbrc.1995.1310openalex-snapshot
Role of THR-252 in Cytochrome P450CAM: A Study with Unnatural Amino Acid Mutagenesis
inferredcites →https://doi.org/10.1006/jmbi.1994.1355openalex-snapshot
Crystallization and Preliminary X-ray Diffraction Studies of Nitric Oxide Reductase Cytochrome P450nor from Fusarium oxysporum
inferredcites →https://doi.org/10.1007/978-1-4613-9783-0openalex-snapshot
Active Oxygen in Biochemistry
inferredcites →https://doi.org/10.1007/978-1-4615-3874-5_31openalex-snapshot
Kinetic Basis for the Impaired Oxygenation of Eicosapentaenoate by Prostaglandin Endoperoxide Synthase
inferredcites →https://doi.org/10.1007/bf01990503openalex-snapshot
Interferons and indoleamine 2,3-dioxygenase: Role in antimicrobial and antitumor effects
inferredcites →https://doi.org/10.1007/bfb0019663openalex-snapshot
Cytochrome P450 and biological hydroxylation reactions
inferredcites →https://doi.org/10.1016/0003-9861(58)90095-xopenalex-snapshot
Studies on pig liver microsomes. I. Enzymic and pigment composition of different microsomal fractions
inferredcites →https://doi.org/10.1016/0003-9861(58)90436-3openalex-snapshot
Pigments of rat liver microsomes
inferredcites →https://doi.org/10.1016/0003-9861(67)90256-1openalex-snapshot
Enzymic formation of d-kynurenine from d-tryptophan
inferredcites →https://doi.org/10.1016/0003-9861(69)90401-9openalex-snapshot
The microsomal oxygenation of ethyl benzene: Isotopic, stereochemical, and induction studies
inferredcites →https://doi.org/10.1016/0003-9861(86)90567-9openalex-snapshot
The oxidation of arachidonic acid by the cyclooxygenase activity of purified prostaglandin H synthase: Spin trapping of a carbon-centered free radical intermediate
inferredcites →https://doi.org/10.1016/0003-9861(87)90560-1openalex-snapshot
Utilization of dihydroflavin mononucleotide and superoxide anion for the decyclization of l-tryptophan by murine epididymal indoleamine 2,3-dioxygenase
inferredcites →https://doi.org/10.1016/0003-9861(89)90034-9openalex-snapshot
Kinetic deuterium isotope effects on deamination and N-hydroxylation of cyclohexylamine by rabbit liver microsomes
inferredcites →https://doi.org/10.1016/0003-9861(91)90142-6openalex-snapshot
1-methyl-dl-tryptophan, β-(3-benzofuranyl)-dl-alanine (the oxygen analog of tryptophan), and β-[3-benzo(b)thienyl]-dl-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase
inferredcites →https://doi.org/10.1016/0003-9861(92)90468-copenalex-snapshot
Cytochrome P450cam-catalyzed oxidation of a hypersensitive radical probe
inferredcites →https://doi.org/10.1016/0005-2760(91)90119-3openalex-snapshot
Prostaglandin endoperoxide synthase: structure and catalysis
inferredcites →https://doi.org/10.1016/0005-2795(76)90118-5openalex-snapshot
One electron reduction of metmyoglobin and methemoglobin and the reaction of the reduced molecule with oxygen
inferredcites →https://doi.org/10.1016/0006-291x(71)90591-2openalex-snapshot
The mechanism of the oxidation of d-amphetamine by rabbit liver oxygenase. Oxygen-18 studies
inferredcites →https://doi.org/10.1016/0006-291x(72)90473-1openalex-snapshot
Primary amines as uncouplers of electron transport from hydroxylation in the secondary-amine mono-oxygenase system of Pseudomonas aminovorans
inferredcites →https://doi.org/10.1016/0006-291x(72)90949-7openalex-snapshot
New degradative routes of 5-hydroxytryptophan and serotonin by intestinal tryptophan 2,3-dioxygenase
inferredcites →https://doi.org/10.1016/0006-291x(76)90646-xopenalex-snapshot
Evidence for the involvement of cytochrome P-450 in reduction of benzo(a)pyrene 4,5-oxide by rat liver microsomes
inferredcites →https://doi.org/10.1016/0006-291x(76)90684-7openalex-snapshot
Spectral intermediates in the reaction of oxygen with purified liver microsomal cytochrome P-450
inferredcites →https://doi.org/10.1016/0006-291x(77)90758-6openalex-snapshot
Intramolecular determination of primary kinetic isotope effects in hydroxylations catalyzed by cytochrome P-450
inferredcites →https://doi.org/10.1016/0006-291x(78)91643-1openalex-snapshot
Aliphatic hydroxylation by highly purified liver microsomal cytochrome P-450. Evidence for a carbon radical intermediate
inferredcites →https://doi.org/10.1016/0006-291x(79)90210-9openalex-snapshot
Electron transfer from pyridinyl radicals, hydrated electrons, CO2•- and O2•- bacterial cytochrome P450
inferredcites →https://doi.org/10.1016/0006-291x(80)90535-5openalex-snapshot
Spectrum of chloroperoxidase compound I
inferredcites →https://doi.org/10.1016/0006-291x(80)91266-8openalex-snapshot
Steric considerations regarding the biodegradation of cholesterol to pregnenolone.-exclusion of (22S)-22-hydroxycholesterol and 22-ketocholesterol as intermediates
inferredcites →https://doi.org/10.1016/0006-291x(82)91589-3openalex-snapshot
Source of oxygen in cytochrome P-450 catalyzed carbinolamine formation
inferredcites →https://doi.org/10.1016/0006-291x(90)91256-ropenalex-snapshot
Deduced primary structure of rat tryptophan-2,3-dioxygenase
inferredcites →https://doi.org/10.1016/0006-291x(90)91666-gopenalex-snapshot
Molecular cloning, sequencing and expression of human interferon-γ-inducible indoleamine 2,3-dioxygenase cDNA
inferredcites →https://doi.org/10.1016/0006-291x(92)91828-eopenalex-snapshot
Importance of histidine residue 25 of rat heme oxygenase for its catalytic activity
inferredcites →https://doi.org/10.1016/0006-291x(92)92357-4openalex-snapshot
Mouse hepatic microsomal oxidation of aliphatic aldehydes (C8 to C011) to carboxylic acids
inferredcites →https://doi.org/10.1016/0006-2952(67)90298-5openalex-snapshot
Studies on the mechanism of action of mammalian hepatic azoreductase—II
inferredcites →https://doi.org/10.1016/0006-2952(74)90008-2openalex-snapshot
Microsomal epoxidation of cis-stilbene: Decrease in epoxidase activity related to lipid peroxidation
inferredcites →https://doi.org/10.1016/0006-2952(74)90058-6openalex-snapshot
Photometric assay of hepatic epoxide hydrolase activity with safrole oxide (SAFO) as substrate
inferredcites →https://doi.org/10.1016/0006-2952(79)90251-xopenalex-snapshot
Reactions of trichloroethylene epoxide in aqueous systems
inferredcites →https://doi.org/10.1016/0014-5793(78)80206-3openalex-snapshot
Reconstitution of benzo[a] pyrene 4,5‐oxide reductase activity by purified cytochrome P‐450
inferredcites →https://doi.org/10.1016/0014-5793(83)80505-5openalex-snapshot
Absorption spectra of cytochrome P450CAM in the reaction with peroxy acids
inferredcites →https://doi.org/10.1016/0014-5793(84)80189-1openalex-snapshot
EPR titration of ovine prostaglandin H synthase with hemin
inferredcites →https://doi.org/10.1016/0014-5793(91)81398-ropenalex-snapshot
EPR‐spectroscopy of reduced oxyferrous‐P450cam
inferredcites →https://doi.org/10.1016/0022-2836(87)90190-2openalex-snapshot
HIGH-RESOLUTION CRYSTAL STRUCTURE OF CYTOCHROME P450-CAM
inferredcites →https://doi.org/10.1016/0022-2836(94)90019-1openalex-snapshot
Crystal structure and refinement of cytochrome P450terp at 2·3 Å resolution
inferredcites →https://doi.org/10.1016/0040-4020(67)85151-2openalex-snapshot
The proton dissociation constant of pyrrole, indole and related compounds
inferredcites →https://doi.org/10.1016/0162-0134(89)84492-7openalex-snapshot
Effects of tryptophan analogs on the catalytic activity of indoleamine 2,3-dioxygenase
inferredcites →https://doi.org/10.1016/0163-7258(91)90020-mopenalex-snapshot
The involvement of free radicals in the mechanisms of monooxygenases
inferredcites →https://doi.org/10.1016/0163-7258(91)90054-popenalex-snapshot
Prostaglandin and thromboxane biosynthesis
inferredcites →https://doi.org/10.1016/0163-7258(92)90015-ropenalex-snapshot
The approach to understanding aromatic hydrocarbon carcinogenesis. The central role of radical cations in metabolic activation
inferredcites →https://doi.org/10.1016/0165-6147(89)90007-2openalex-snapshot
Cytochrome P-450 catalysis: radical intermediates and dehydrogenation reactions
inferredcites →https://doi.org/10.1016/0167-4838(84)90202-4openalex-snapshot
Extensive studies of the heme coordination structure of indoleamine 2,3-dioxygenase and of tryptophan binding with magnetic and natural circular dichroism and electron paramagnetic resonance spectroscopy
inferredcites →https://doi.org/10.1016/0167-4838(87)90249-4openalex-snapshot
Electron paramagnetic resonance and spectrophotometric studies of the peroxide compounds of manganese-substituted horseradish peroxidase, cytochrome-c peroxidase and manganese-porphyrin model complexes
inferredcites →https://doi.org/10.1016/0167-4838(89)90071-xopenalex-snapshot
Kinetics of the reaction of superoxide anion with ferric horseradish peroxidase
inferredcites →https://doi.org/10.1016/0167-4838(96)00031-3openalex-snapshot
Ligation of the iron in the heme-heme oxygenase complex: X-ray absorption, electronic absorption and magnetic circular dichroism studies
inferredcites →https://doi.org/10.1016/0304-5102(80)85025-5openalex-snapshot
Reaction of indoles with molecular oxygen catalyzed by metalloporphyrins
inferredcites →https://doi.org/10.1016/0378-1119(91)90154-4openalex-snapshot
Cloning and expression of a cDNA encoding mouse indoleamine 2,3-dioxygenase
inferredcites →https://doi.org/10.1016/0960-0760(93)90240-wopenalex-snapshot
Studies on the mechanism of aromatase and other cytochrome P450 mediated deformylation reactions
inferredcites →https://doi.org/10.1016/0960-0760(93)90241-nopenalex-snapshot
Mechanistic studies on aromatase and related CC bond cleaving P-450 enzymes
inferredcites →https://doi.org/10.1016/0960-894x(95)00486-dopenalex-snapshot
The mechanism of aromatase — a molecular modelling perspective
inferredcites →https://doi.org/10.1016/0968-0004(76)90037-2openalex-snapshot
Porphyrins and metalloporphyrins
inferredcites →https://doi.org/10.1016/0968-0004(87)90123-xopenalex-snapshot
The two redox potentials for oxygen reduction to superoxide
inferredcites →https://doi.org/10.1016/b978-0-12-220107-3.50013-xopenalex-snapshot
Peroxidases, Catalases, and Chloroperoxidase
inferredcites →https://doi.org/10.1016/b978-1-4831-0093-7.50008-5openalex-snapshot
SEQUENTIAL ELECTRON TRANSFER REACTIONS CATALYZED BY CYTOCHROME P-450 ENZYMES
inferredcites →https://doi.org/10.1016/s0010-8545(00)80316-1openalex-snapshot
On the function and mechanism of action of peroxidases
inferredcites →https://doi.org/10.1016/s0020-1693(00)80454-5openalex-snapshot
Important role of Fe(III)TPP-oxygen-skatole ternary complex in tryptophan dioxygenase model reaction system
inferredcites →https://doi.org/10.1016/s0020-1693(00)84305-4openalex-snapshot
Models for ferrous cytochrome b5: Sign inversions in the magnetic circular dichroism spectra of bis-imidazole ferrous porphyrin systems
inferredcites →https://doi.org/10.1016/s0021-9258(17)30036-4openalex-snapshot
Purification and properties of heme oxygenase from rat liver microsomes.
inferredcites →https://doi.org/10.1016/s0021-9258(17)30447-7openalex-snapshot
Indoleamine 2,3-dioxygenase. Purification and some properties
inferredcites →https://doi.org/10.1016/s0021-9258(17)31235-8openalex-snapshot
On the mechanism of prostacyclin and thromboxane A2 biosynthesis
inferredcites →https://doi.org/10.1016/s0021-9258(17)31418-7openalex-snapshot
The respiratory burst oxidase.
inferredcites →https://doi.org/10.1016/s0021-9258(17)32750-3openalex-snapshot
Nature of the free radical in ribonucleotide reductase from Escherichia coli.
inferredcites →https://doi.org/10.1016/s0021-9258(17)33098-3openalex-snapshot
Purification of the cyclooxygenase that forms prostaglandins. Demonstration of two forms of iron in the holoenzyme.
inferredcites →https://doi.org/10.1016/s0021-9258(17)33534-2openalex-snapshot
Purification of prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes.
inferredcites →https://doi.org/10.1016/s0021-9258(17)33687-6openalex-snapshot
Binding of nitric oxide to reduced L-tryptophan-2,3-dioxygenase as studied by electron paramagnetic resonance.
inferredcites →https://doi.org/10.1016/s0021-9258(17)34657-4openalex-snapshot
Prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes. Inactivation and activation by heme and other metalloporphyrins.
inferredcites →https://doi.org/10.1016/s0021-9258(17)34707-5openalex-snapshot
Purification and properties of heme oxygenase from pig spleen microsomes.
inferredcites →https://doi.org/10.1016/s0021-9258(17)35913-6openalex-snapshot
Binding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenases.
inferredcites →https://doi.org/10.1016/s0021-9258(17)36209-9openalex-snapshot
The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.
inferredcites →https://doi.org/10.1016/s0021-9258(17)37493-8openalex-snapshot
Interaction between peroxidase and cyclooxygenase activities in prostaglandin-endoperoxide synthase. Interpretation of reaction kinetics.
inferredcites →https://doi.org/10.1016/s0021-9258(17)37999-1openalex-snapshot
The tyrosine free radical in ribonucleotide reductase from Escherichia coli.
inferredcites →https://doi.org/10.1016/s0021-9258(17)40208-0openalex-snapshot
Indoleamine 2,3-dioxygenase. Characterization and properties of enzyme. O2- complex.
inferredcites →https://doi.org/10.1016/s0021-9258(17)40524-2openalex-snapshot
Intracellular utilization of superoxide anion by indoleamine 2,3-dioxygenase of rabbit enterocytes.
inferredcites →https://doi.org/10.1016/s0021-9258(17)41772-8openalex-snapshot
A role for Asp-251 in cytochrome P-450cam oxygen activation.
inferredcites →https://doi.org/10.1016/s0021-9258(17)42212-5openalex-snapshot
Heme-heme oxygenase complex. Structure of the catalytic site and its implication for oxygen activation.
inferredcites →https://doi.org/10.1016/s0021-9258(17)42488-4openalex-snapshot
Characterization of two constitutive forms of rat liver microsomal heme oxygenase. Only one molecular species of the enzyme is inducible.
inferredcites →https://doi.org/10.1016/s0021-9258(17)43062-6openalex-snapshot
The reaction of superoxide radical with catalase. Mechanism of the inhibition of catalase by superoxide radical.
inferredcites →https://doi.org/10.1016/s0021-9258(17)43248-0openalex-snapshot
Kinetic isotope effects on cytochrome P-450-catalyzed oxidation reactions. The oxidative O-dealkylation of 7-ethoxycoumarin.
inferredcites →https://doi.org/10.1016/s0021-9258(17)43882-8openalex-snapshot
The use of intramolecular isotope effects to distinguish between deprotonation and hydrogen atom abstraction mechanisms in cytochrome P-450- and peroxidase-catalyzed N-demethylation reactions.
inferredcites →https://doi.org/10.1016/s0021-9258(17)44644-8openalex-snapshot
Functional differences between peroxidase compound I and the cytochrome P-450 reactive oxygen intermediate.
inferredcites →https://doi.org/10.1016/s0021-9258(17)46773-1openalex-snapshot
Isotope effects and alternative substrate reactivities for tryptophan 2,3-dioxygenase.
inferredcites →https://doi.org/10.1016/s0021-9258(18)31375-9openalex-snapshot
Nitric oxide synthase structure and mechanism
inferredcites →https://doi.org/10.1016/s0021-9258(18)32606-1openalex-snapshot
The cytochrome P-450 active site. Regiospecificity of prosthetic heme alkylation by olefins and acetylenes.
inferredcites →https://doi.org/10.1016/s0021-9258(18)32957-0openalex-snapshot
Magnetic and natural circular dichroism of L-tryptophan 2,3-dioxygenases and indoleamine 2,3-dioxygenase. I. Spectra of ferric and ferrous high spin forms.
inferredcites →https://doi.org/10.1016/s0021-9258(18)33756-6openalex-snapshot
The catalytic mechanism of cytochrome P-450. Spin-trapping evidence for one-electron substrate oxidation.
inferredcites →https://doi.org/10.1016/s0021-9258(18)34332-1openalex-snapshot
Sulfur donor ligand binding to ferric cytochrome P-450-CAM and myoglobin. Ultraviolet-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopic investigation of the complexes.
inferredcites →https://doi.org/10.1016/s0021-9258(18)34449-1openalex-snapshot
Purification and properties of bovine spleen heme oxygenase. Amino acid composition and sites of action of inhibitors of heme oxidation.
inferredcites →https://doi.org/10.1016/s0021-9258(18)38093-1openalex-snapshot
Lanosterol 14 alpha-methyl demethylase. Isolation and characterization of the third metabolically generated oxidative demethylation intermediate.
inferredcites →https://doi.org/10.1016/s0021-9258(18)41536-0openalex-snapshot
Rat liver heme oxygenase. High level expression of a truncated soluble form and nature of the meso-hydroxylating species.
inferredcites →https://doi.org/10.1016/s0021-9258(18)43699-xopenalex-snapshot
Kinetic isotope effects in cytochrome P-450-catalyzed oxidation reactions. Intermolecular and intramolecular deuterium isotope effects during the N-demethylation of N,N-dimethylphentermine.
inferredcites →https://doi.org/10.1016/s0021-9258(18)43731-3openalex-snapshot
Evidence for a peroxide-initiated free radical mechanism of prostaglandin biosynthesis.
inferredcites →https://doi.org/10.1016/s0021-9258(18)43915-4openalex-snapshot
Heme oxygenase (HO-1). Evidence for electrophilic oxygen addition to the porphyrin ring in the formation of alpha-meso-hydroxyheme.
inferredcites →https://doi.org/10.1016/s0021-9258(18)45592-5openalex-snapshot
One-electron reduction of the oxyform of 2,4-diacetyldeuterocytochrome P-450cam.
inferredcites →https://doi.org/10.1016/s0021-9258(18)48315-9openalex-snapshot
Nucleotide sequence and organization of the rat heme oxygenase gene.
inferredcites →https://doi.org/10.1016/s0021-9258(18)49902-4openalex-snapshot
Oxygenation mechanism in conversion of aldehyde to carboxylic acid catalyzed by a cytochrome P-450 isozyme.
inferredcites →https://doi.org/10.1016/s0021-9258(18)50024-7openalex-snapshot
Coordination structure of the ferric heme iron in engineered distal histidine myoglobin mutants
inferredcites →https://doi.org/10.1016/s0021-9258(18)50757-2openalex-snapshot
Indoleamine 2,3-dioxygenase. Kinetic studies on the binding of superoxide anion and molecular oxygen to enzyme.
inferredcites →https://doi.org/10.1016/s0021-9258(18)52911-2openalex-snapshot
Heme coordination of prostaglandin H synthase.
inferredcites →https://doi.org/10.1016/s0021-9258(18)53102-1openalex-snapshot
Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor.
inferredcites →https://doi.org/10.1016/s0021-9258(18)54889-4openalex-snapshot
Electron spin resonance investigation of tyrosyl radicals of prostaglandin H synthase. Relation to enzyme catalysis.
inferredcites →https://doi.org/10.1016/s0021-9258(18)60893-2openalex-snapshot
Purification to homogeneity and initial physical characterization of secondary amine monooxygenase.
inferredcites →https://doi.org/10.1016/s0021-9258(18)60993-7openalex-snapshot
Heme spin states and peroxide-induced radical species in prostaglandin H synthase.
inferredcites →https://doi.org/10.1016/s0021-9258(18)62232-xopenalex-snapshot
The Effects of Protein Conformation on the Heme Symmetry in High Spin Ferric Heme Proteins as Studied by Electron Paramagnetic Resonance
inferredcites →https://doi.org/10.1016/s0021-9258(18)62967-9openalex-snapshot
The Oxygenated Form of l-Tryptophan 2,3-Dioxygenase as Reaction Intermediate
inferredcites →https://doi.org/10.1016/s0021-9258(18)63477-5openalex-snapshot
Microsomal Heme Oxygenase
inferredcites →https://doi.org/10.1016/s0021-9258(18)63506-9openalex-snapshot
The Stereochemistry of Tritium at Carbon Atoms 1, 7, and 15 in Cholesterol Derived from (3R,2R)-(2-3H)-Mevalonic Acid
inferredcites →https://doi.org/10.1016/s0021-9258(18)68457-1openalex-snapshot
Cytochrome P-450-catalyzed dehydrogenation of 1,4-dihydropyridines.
inferredcites →https://doi.org/10.1016/s0021-9258(18)69078-7openalex-snapshot
Evidence suggesting that the two forms of heme oxygenase are products of different genes.
inferredcites →https://doi.org/10.1016/s0021-9258(18)71630-xopenalex-snapshot
Alkylaryl sulfides as Peroxidase Reducing Substrates for Prostaglandin H Synthase
inferredcites →https://doi.org/10.1016/s0021-9258(18)81216-9openalex-snapshot
The Mechanism of Metmyoglobin Oxidation
inferredcites →https://doi.org/10.1016/s0021-9258(18)82162-7openalex-snapshot
Partitioning between N-dealkylation and N-oxygenation in the oxidation of N,N-dialkylarylamines catalyzed by cytochrome P450 2B1
inferredcites →https://doi.org/10.1016/s0021-9258(18)91383-9openalex-snapshot
The Interaction of Porphyrins and Metalloporphyrins with Apocytochrome b5
inferredcites →https://doi.org/10.1016/s0021-9258(18)92717-1openalex-snapshot
Cytochrome P-450. Multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms
inferredcites →https://doi.org/10.1016/s0021-9258(18)93665-3openalex-snapshot
Studies on Cytochrome c Peroxidase
inferredcites →https://doi.org/10.1016/s0021-9258(18)94231-6openalex-snapshot
The Roles of Superoxide Anion and Methylene Blue in the Reductive Activation of Indoleamine 2,3-Dioxygenase by Ascorbic Acid or by Xanthine Oxidase-Hypoxanthine
inferredcites →https://doi.org/10.1016/s0021-9258(18)95676-0openalex-snapshot
Spectral properties of the higher oxidation states of prostaglandin H synthase.
inferredcites →https://doi.org/10.1016/s0021-9258(18)96096-5openalex-snapshot
Studies on Cytochrome c Peroxidase
inferredcites →https://doi.org/10.1016/s0021-9258(18)99130-1openalex-snapshot
Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction
inferredcites →https://doi.org/10.1016/s0021-9258(18)99420-2openalex-snapshot
Tryptophan Pyrrolase of Rabbit Intestine
inferredcites →https://doi.org/10.1016/s0021-9258(18)99433-0openalex-snapshot
On the Mechanism of the Biosynthesis of Prostaglandins E1 and F1α
inferredcites →https://doi.org/10.1016/s0021-9258(19)34105-5openalex-snapshot
The aspirin and heme-binding sites of ovine and murine prostaglandin endoperoxide synthases.
inferredcites →https://doi.org/10.1016/s0021-9258(19)35424-9openalex-snapshot
Single turnover kinetics of the reaction between oxycytochrome P-450cam and reduced putidaredoxin.
inferredcites →https://doi.org/10.1016/s0021-9258(19)37092-9openalex-snapshot
Prostaglandin H synthase kinetics. The effect of substituted phenols on cyclooxygenase activity and the substituent effect on phenolic peroxidatic activity.
inferredcites →https://doi.org/10.1016/s0021-9258(19)37108-xopenalex-snapshot
Prostaglandin H synthase. Kinetics of tyrosyl radical formation and of cyclooxygenase catalysis.
inferredcites →https://doi.org/10.1016/s0021-9258(19)40689-3openalex-snapshot
Mass spectrometric study of the enzymatic conversion of cholesterol to (22R)-22-hydroxycholesterol, (20R,22R)-20,22-dihydroxycholesterol, and pregnenolone, and of (22R)-22-hydroxycholesterol to the lgycol and pregnenolone in bovine adrenocortical preparations. Mode of oxygen incorporation
inferredcites →https://doi.org/10.1016/s0021-9258(19)45449-5openalex-snapshot
Electromagnetic Properties of Hemoproteins
inferredcites →https://doi.org/10.1016/s0021-9258(19)45795-5openalex-snapshot
ω-Oxidation of Fatty Acids
inferredcites →https://doi.org/10.1016/s0021-9258(19)47085-3openalex-snapshot
Spectroscopic Characterization of Secondary Amine Mono-oxygenase
inferredcites →https://doi.org/10.1016/s0021-9258(19)69049-6openalex-snapshot
N-Alkylprotoporphyrin IX formation in 3,5-dicarbethoxy-1,4-dihydrocollidine-treated rats. Transfer of the alkyl group from the substrate to the porphyrin.
inferredcites →https://doi.org/10.1016/s0021-9258(19)69271-9openalex-snapshot
On the mechanism of action of cytochrome P-450. Role of peroxy spectral intermediates in substrate hydroxylation.
inferredcites →https://doi.org/10.1016/s0021-9258(19)69459-7openalex-snapshot
Mechanism of estrogen biosynthesis. Stereochemistry of C-1 hydrogen elimination in the aromatization of 2 beta-hydroxy-19-oxoandrostenedione.
inferredcites →https://doi.org/10.1016/s0021-9258(19)69554-2openalex-snapshot
Structural implication of the heme-linked ionization of horseradish peroxidase probed by the Fe-histidine stretching Raman line.
inferredcites →https://doi.org/10.1016/s0021-9258(19)70217-8openalex-snapshot
Acid-alkaline transition and thermal spin equilibrium of the heme in ferric L-tryptophan 2,3-dioxygenases.
inferredcites →https://doi.org/10.1016/s0021-9258(19)70741-8openalex-snapshot
A carbon-centered free radical intermediate in the prostaglandin synthetase oxidation of arachidonic acid. Spin trapping and oxygen uptake studies.
inferredcites →https://doi.org/10.1016/s0021-9258(19)77982-4openalex-snapshot
Mechanism of interferon-gamma action. Characterization of indoleamine 2,3-dioxygenase in cultured human cells induced by interferon-gamma and evaluation of the enzyme-mediated tryptophan degradation in its anticellular activity.
inferredcites →https://doi.org/10.1016/s0021-9258(19)83805-xopenalex-snapshot
Formation of low spin complexes of ferric cytochrome P-450-CAM with anionic ligands. Spin state and ligand affinity comparison to myoglobin.
inferredcites →https://doi.org/10.1016/s0021-9258(19)84822-6openalex-snapshot
Effects of tryptophan and pH on the kinetics of superoxide radical binding to indoleamine 2,3-dioxygenase studied by pulse radiolysis
inferredcites →https://doi.org/10.1016/s0021-9258(19)85506-0openalex-snapshot
Oxygenated form of heme . heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex.
inferredcites →https://doi.org/10.1016/s0021-9258(19)85568-0openalex-snapshot
An electron paramagnetic resonance study of the high and low spin forms of chloroperoxidase.
inferredcites →https://doi.org/10.1016/s0021-9258(19)85598-9openalex-snapshot
Copper is not essential for the catalytic activity of L-tryptophan 2,3-dioxygenase.
inferredcites →https://doi.org/10.1016/s0021-9258(19)85639-9openalex-snapshot
On the mechanism of action of cytochrome P-450. Spectral intermediates in the reaction of P-450LM2 with peroxy compounds.
inferredcites →https://doi.org/10.1016/s0021-9258(19)86035-0openalex-snapshot
Indoleamine 2,3-dioxygenase. Equilibrium studies of the tryptophan binding to the ferric, ferrous, and CO-bound enzymes.
inferredcites →https://doi.org/10.1016/s0021-9258(19)86816-3openalex-snapshot
The oxidation-reduction potentials of compound I/compound II and compound II/ferric couples of horseradish peroxidases A2 and C.
inferredcites →https://doi.org/10.1016/s0021-9258(19)89213-xopenalex-snapshot
Characterization of rat and human liver microsomal cytochrome P-450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism.
inferredcites →https://doi.org/10.1016/s0021-9258(20)82149-8openalex-snapshot
Prostaglandin H synthase. Stoichiometry of heme cofactor.
inferredcites →https://doi.org/10.1016/s0021-9258(20)82244-3openalex-snapshot
The Carbon Monoxide-binding Pigment of Liver Microsomes
inferredcites →https://doi.org/10.1016/s0026-895x(25)10767-0openalex-snapshot
Reduction of Tertiary Amine N-Oxides by Liver Microsomal Cytochrome P-450
inferredcites →https://doi.org/10.1016/s0026-895x(25)13029-0openalex-snapshot
Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase.
inferredcites →https://doi.org/10.1016/s0031-6997(25)07235-7openalex-snapshot
MECHANISMS OF CHEMICAL CARCINOGENESIS: NATURE OF PROXIMATE CARCINOGENS AND INTERACTIONS WITH MACROMOLECULES
inferredcites →https://doi.org/10.1016/s0040-4020(01)85808-7openalex-snapshot
Competition Methods and Scales for Alkyl Radical Reaction Kinetics
inferredcites →https://doi.org/10.1016/s0040-4039(00)81368-4openalex-snapshot
Mechanism of Co(salen)-catalyzed oxygenolysis of indole ring as a model for the tryptophan-2,3-dioxygenase reaction
inferredcites →https://doi.org/10.1016/s0040-4039(00)86881-1openalex-snapshot
One electron transfer mechanism in the enzymatic oxygenation of sulfoxide to sulfone promoted by a reconstituted system with purified cytochrome p-450
inferredcites →https://doi.org/10.1016/s0076-6879(78)52019-3openalex-snapshot
[17] Bacterial P-450cam methylene monooxygenase components: Cytochrome m, putidaredoxin, and putidaredoxin reductase
inferredcites →https://doi.org/10.1016/s0969-2126(01)00274-xopenalex-snapshot
The crystal structure of chloroperoxidase: a heme peroxidase–cytochrome P450 functional hybrid
inferredcites →https://doi.org/10.1016/s1874-6047(08)60027-xopenalex-snapshot
9 Molecular Mechanism of Oxygen Activation by P-450
inferredcites →https://doi.org/10.1021/ar00019a007openalex-snapshot
Mechanism of alkene epoxidation by iron, chromium, and manganese higher valent oxo-metalloporphyrins
inferredcites →https://doi.org/10.1021/ar00139a003openalex-snapshot
Heme catabolism: a new look at substrates and enzymes
inferredcites →https://doi.org/10.1021/ar50117a006openalex-snapshot
Peroxidic intermediates in photosensitized oxygenation of tryptophan derivatives
inferredcites →https://doi.org/10.1021/ar50154a003openalex-snapshot
Spin-pairing model of dioxygen binding and its application to various transition-metal systems as well as hemoglobin cooperativity
inferredcites →https://doi.org/10.1021/ba-1971-0100.ch013openalex-snapshot
Low—Spin Compounds of Heme Proteins
inferredcites →https://doi.org/10.1021/bi00013a034openalex-snapshot
Expression and characterization of truncated human heme oxygenase (hHO-1) and a fusion protein of hHO-1 with human cytochrome P450 reductase
inferredcites →https://doi.org/10.1021/bi00026a034openalex-snapshot
Comparison of branched-chain and tightly coupled reaction mechanisms for prostaglandin H synthase
inferredcites →https://doi.org/10.1021/bi00028a014openalex-snapshot
Iron-Ligand Structure and Iron Redox Property of Nitric Oxide Reductase Cytochrome P450nor from Fusarium oxysporum: Relevance to Its NO Reduction Activity
inferredcites →https://doi.org/10.1021/bi00033a021openalex-snapshot
Origin of the pH-Dependent Spectroscopic Properties of Pentacoordinate Metmyoglobin Variants
inferredcites →https://doi.org/10.1021/bi00045a014openalex-snapshot
The role of Thr268 in oxygen activation of cytochrome P450BM-3
inferredcites →https://doi.org/10.1021/bi00052a031openalex-snapshot
Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase
inferredcites →https://doi.org/10.1021/bi00086a028openalex-snapshot
Cytochrome P450 hydroxylation of hydrocarbons: Variation in the rate of oxygen rebound using cyclopropyl radical clocks including two new ultrafast probes
inferredcites →https://doi.org/10.1021/bi00094a009openalex-snapshot
Molecular recognition in cytochrome P-450: Mechanism for the control of uncoupling reactions
inferredcites →https://doi.org/10.1021/bi00116a001openalex-snapshot
Tyrosyl radicals and their role in hydroperoxide-dependent activation and inactivation of prostaglandin endoperoxide synthase
inferredcites →https://doi.org/10.1021/bi00174a027openalex-snapshot
Androgen Formation by Cytochrome P450 CYP17. Solvent Isotope Effect and pL Studies Suggest a Role for Protons in the Regulation of Oxene versus Peroxide Chemistry
inferredcites →https://doi.org/10.1021/bi00180a039openalex-snapshot
Mechanism of the Acyl-Carbon Cleavage and Related Reactions Catalyzed by Multifunctional P-450s: Studies on Cytochrome P-45017.alpha.
inferredcites →https://doi.org/10.1021/bi00184a023openalex-snapshot
Heme-Heme Oxygenase Complex: Structure and Properties of the Catalytic Site from Resonance Raman Scattering
inferredcites →https://doi.org/10.1021/bi00187a008openalex-snapshot
On the Mechanism of Action of Cytochrome P450: Evaluation of Hydrogen Abstraction in Oxygen-Dependent Alcohol Oxidation
inferredcites →https://doi.org/10.1021/bi00187a013openalex-snapshot
Intimate Relation between Cyclooxygenase and Peroxidase Activities of Prostaglandin H Synthase. Peroxidase Reaction of Ferulic Acid and Its Influence on the Reaction of Arachidonic Acid
inferredcites →https://doi.org/10.1021/bi00187a033openalex-snapshot
Proton NMR Investigation of Substrate-Bound Heme Oxygenase: Evidence for Electronic and Steric Contributions to Stereoselective Heme Cleavage
inferredcites →https://doi.org/10.1021/bi00201a009openalex-snapshot
Cytochrome P450-Catalyzed Hydroxylation of Hydrocarbons: Kinetic Deuterium Isotope Effects for the Hydroxylation of an Ultrafast Radical Clock
inferredcites →https://doi.org/10.1021/bi00204a003openalex-snapshot
.delta.-Conotoxin GmVIA, a Novel Peptide from the Venom of Conus gloriamaris
inferredcites →https://doi.org/10.1021/bi00214a012openalex-snapshot
Resonance Raman and EPR spectroscopic studies on heme-heme oxygenase complexes
inferredcites →https://doi.org/10.1021/bi00250a015openalex-snapshot
Aromatization of a Bicyclic Steroid Analog, 3-Oxodecalin-4-ene-10-carboxaldehyde, by Liver Microsomal Cytochrome P450 2B4
inferredcites →https://doi.org/10.1021/bi00250a026openalex-snapshot
Identification of Histidine 25 as the Heme Ligand in Human Liver Heme Oxygenase
inferredcites →https://doi.org/10.1021/bi00293a005openalex-snapshot
Olefin oxidation by cytochrome P-450: evidence for group migration in catalytic intermediates formed with vinylidene chloride and trans-1-phenyl-1-butene
inferredcites →https://doi.org/10.1021/bi00368a038openalex-snapshot
Spectroscopic and equilibrium properties of the indoleamine 2,3-dioxygenase-tryptophan-oxygen ternary complex and of analogous enzyme derivatives. Tryptophan binding to ferrous enzyme adducts with dioxygen, nitric oxide, and carbon monoxide
inferredcites →https://doi.org/10.1021/bi00415a014openalex-snapshot
Heme pocket interactions in cytochrome c peroxidase studied by site-directed mutagenesis and resonance Raman spectroscopy
inferredcites →https://doi.org/10.1021/bi00431a016openalex-snapshot
Oxidation of substituted N,N-dimethylanilines by cytochrome P-450: estimation of the effective oxidation-reduction potential of cytochrome P-450
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What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Metabolome Adaptation and Oxidative Stress Response of Common Carp (Cyprinus Carpio) to Altered Water Pollution Levelsmetabolome Adaptation and Oxidative Stress Response of Common Carp (Cyprinus Carpio) to Altered Water Pollution Levels
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Theoretical modeling of the heme group with a hybrid QM/MM method
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A Square-Planar Dinickel(II) Complex with a Noninnocent Dinucleating Oxamate Ligand: Evidence for a Ligand Radical Species
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Solution Coordination Chemistry of Protohaemin IX Peptide Derivatives
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Cytochrome P-450 model reaction: effects of substitution on the rate of aromatic hydroxylation
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High-valent iron porphyrins
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Heme protein biosensors
inferred← citeshttps://doi.org/10.1002/(sici)1521-3757(19990115)111:1/2<93::aid-ange93>3.0.co;2-popenalex-snapshot
Substrate für schnelle Ladungsübertragung auf redoxaktive Cofaktoren in den aktiven Zentren von Proteinen
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Umwandlung von molekularem Sauerstoff in eine Hydroperoxoverbindung über eine Protonierungs-induzierte Ringöffnung eines cyclischen η2-Peroxo-Intermediats: Charakterisierung der η2-Peroxo- und Hydroperoxokomplexe
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Über den „Neuanbindungs”-Mechanismus der Alkanhydroxylierung durch Cytochrom P450: elektronische Struktur der Zwischenstufe und Charakter des Elektronentransfers bei der Neuanbindung
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Electronic Structure Makes a Difference: Cytochrome P-450 Mediated Hydroxylations of Hydrocarbons as a Two-State Reactivity Paradigm
inferred← citeshttps://doi.org/10.1002/0470028637.met223openalex-snapshot
The Nrf H Cytochrome c Quinol Dehydrogenase
inferred← citeshttps://doi.org/10.1002/0470028637.met257openalex-snapshot
para‐Aminobenzoate N ‐Oxygenase
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Iron: Heme Proteins, Mono‐ & DioxygenasesBased in part on the article Iron: Heme Proteins, Mono‐ & Dioxygenases by Masanori Sono & John H. Dawson which appeared in the Encyclopedia of Inorganic Chemistry, First Edition .
inferred← citeshttps://doi.org/10.1002/0470862106.ia113openalex-snapshot
Iron Proteins with Mononuclear Active Sites
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Selective Oxidation – Homogeneous
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Protein Engineering: Recent Trends
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Metal-Mediated Oxidation of Tertiary Alcohols and Related Fragmentations
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FeIII-Hydroperoxo and Peroxo Complexes with Aminopyridyl Ligands and the Resonance Raman Spectroscopic Identification of the Fe−O and O−O Stretching Modes
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Alkane Hydroxylation by Cytochrome P450: Is Kinetic Isotope Effect a Reliable Probe of Transition State Structure?
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Zwei Reaktionswege beim „Wiederanbindungs”-Mechanismus der Alkanhydroxylierung durch Cytochrom P450: Entstehung freier Radikale mit begrenzter Lebensdauer
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Wasserstoffbrücken-gebundenes Sauerstoffaddukt eines Eisenporphyrins mit Alkanthiolatligand: ein fortgeschrittenes Cytochrom-P450-Modell
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Oxygenation of Hydrocarbons Mediated by Mixed-Valent Basic Iron Trifluoroacetate and Valence-Separated Component Species under Gif-Type Conditions Involves Carbon- and Oxygen-Centered Radicals
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The High-Valent Compound of Cytochrome P450: The Nature of the Fe−S Bond and the Role of the Thiolate Ligand as an Internal Electron Donor
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Dendritisch eingeschlossene aktive Zentren: Anwendung des Isolationsprinzips der Natur in der Biomimetik und den Materialwissenschaften
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Biokatalytisch relevante rautenförmige Bis(μ-oxo)dimetall-Kerne in Kupfer- und Eisenkomplexen
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Interaction between Dioxoruthenium(VI) Porphyrins and Hydroxylamines: Coordination ofN-Substituted Hydroxylamine to Ruthenium and X-ray Crystal Structures of Ruthenium Complexes with a Unidentate Nitrosoarene Ligand
inferred← citeshttps://doi.org/10.1002/1521-3765(20011105)7:21<4674::aid-chem4674>3.0.co;2-lopenalex-snapshot
The Reaction of Permanganyl Chloride with Olefins: Intermediates and Mechanism as Derived from Matrix-Isolation Studies and Density Functional Theory Calculations
inferred← citeshttps://doi.org/10.1002/1521-3765(20020402)8:7<1554::aid-chem1554>3.0.co;2-ropenalex-snapshot
Dendritic Ruthenium Porphyrins: A New Class of Highly Selective Catalysts for Alkene Epoxidation and Cyclopropanation
inferred← citeshttps://doi.org/10.1002/1521-3765(20020503)8:9<2067::aid-chem2067>3.0.co;2-vopenalex-snapshot
Isolation of an Oxomanganese(V) Porphyrin Intermediate in the Reaction of a Manganese(III) Porphyrin Complex and H2O2 in Aqueous Solution
inferred← citeshttps://doi.org/10.1002/1521-3773(20000703)39:13<2343::aid-anie2343>3.0.co;2-topenalex-snapshot
Oxygenation of Hydrocarbons Mediated by Mixed-Valent Basic Iron Trifluoroacetate and Valence-Separated Component Species under Gif-Type Conditions Involves Carbon- and Oxygen-Centered Radicals
inferred← citeshttps://doi.org/10.1002/1521-3773(20001103)39:21<3851::aid-anie3851>3.0.co;2-9openalex-snapshot
The High-Valent Compound of Cytochrome P450: The Nature of the Fe−S Bond and the Role of the Thiolate Ligand as an Internal Electron Donor
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Dendritic Encapsulation of Function: Applying Nature's Site Isolation Principle from Biomimetics to Materials Science
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Bis(μ-oxo)dimetal “Diamond” Cores in Copper and Iron Complexes Relevant to Biocatalysis
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Investigating the roles of T224 and T232 in the oxidation of cinnamaldehyde catalyzed by myxobacterial CYP 260B1
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The heme auxotroph Caenorhabditis elegans can cleave the thioether bonds of c‐type cytochromes
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Cytochrome P450 Monooxygenases, Chemistry of
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The Aromatic Amino Acid Hydroxylases
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Oxygen Activation Chemistry of Pacman and Hangman Porphyrin Architectures Based on Xanthene and Dibenzofuran Spacers
inferred← citeshttps://doi.org/10.1002/9780470144428.ch9openalex-snapshot
Bispidine Coordination Chemistry
inferred← citeshttps://doi.org/10.1002/9780470463772.ch18openalex-snapshot
Metalloporphyrin Catalysts of Oxygen Reduction
inferred← citeshttps://doi.org/10.1002/9780470682531.pat0542openalex-snapshot
Catalytic Enantioselective Reactions using Organomanganese Compounds
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Phenoxyl Radical–Metal Complexes
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Recent Advances in the Field of Phenoxyl Radical–Metal Complexes
inferred← citeshttps://doi.org/10.1002/9780470711828.ch4openalex-snapshot
Catalytic CH Bond Activation Reactions
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Reactive Oxygen Species in the Induction of Toxicity
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Metabolic Engineering for the Development and Manufacturing of Pharmaceuticals
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Oxidative Drug Metabolism by Mammalian Cytochrome P450 Enzymes Using Their Monooxygenase and Peroxygenase Functions
inferred← citeshttps://doi.org/10.1002/9781118354377.ch6openalex-snapshot
Nanostructures and Electron‐Transfer Functions of Nonplanar Porphyrins
inferred← citeshttps://doi.org/10.1002/9781118409343.ch1openalex-snapshot
Enzymes Involved in Redox Reactions: Natural Sources and Mechanistic Overview
inferred← citeshttps://doi.org/10.1002/9781118409343.ch4openalex-snapshot
Reactions Involving Oxygenases
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Nature's Strategy For Oxidizing Tryptophan: EPR and Mössbauer Characterization of The Unusual High‐Valent Heme Fe Intermediates
inferred← citeshttps://doi.org/10.1002/9781118754887.ch14openalex-snapshot
Selective Oxidation of Aromatic Rings
inferred← citeshttps://doi.org/10.1002/9781118828083.ch13openalex-snapshot
Biocatalytic Epoxidation for Green Synthesis
inferred← citeshttps://doi.org/10.1002/9781118898277.ch9openalex-snapshot
Catalytic Function and Mechanism of Heme and Nonheme Iron(IV)–Oxo Complexes in Nature
inferred← citeshttps://doi.org/10.1002/9781119129301.ch14openalex-snapshot
Spin States in Iron Porphyrins
inferred← citeshttps://doi.org/10.1002/9781119129301.ch16openalex-snapshot
Heme Proteins – Structure and Function
inferred← citeshttps://doi.org/10.1002/9781119304197.ch16openalex-snapshot
The Recent Developments of Enzymatic Oxidation
inferred← citeshttps://doi.org/10.1002/9781119379256.ch15openalex-snapshot
Selective Oxidation of Alkanes by Metallo‐Monooxygenases and Their Nanobiomimetics
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0099openalex-snapshot
Iron: Heme Proteins, Mono‐ & DioxygenasesBased in part on the article Iron: Heme Proteins, Mono‐ & Dioxygenases by Masanori Sono & John H. Dawson which appeared in theEncyclopedia of Inorganic Chemistry, First Edition.
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0104openalex-snapshot
Iron Porphyrin Chemistry
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0106openalex-snapshot
Iron Proteins with Mononuclear Active Sites
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0314openalex-snapshot
Freeze‐Quench Kinetics
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0650openalex-snapshot
Indoleamine 2,3‐Dioxygenase and Tryptophan 2,3‐Dioxygenase
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0675openalex-snapshot
para‐Aminobenzoate N ‐Oxygenase
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc2276openalex-snapshot
Dye‐Decolorizing Peroxidase ( DyP )
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc2622openalex-snapshot
Heme‐Dependent Oxidative N‐Demethylase
inferred← citeshttps://doi.org/10.1002/9783527611249.ch24openalex-snapshot
Life Science Applications of Fukui Functions
inferred← citeshttps://doi.org/10.1002/9783527613700.ch18openalex-snapshot
Dioxygen and alkane activation by iron‐containing enzymes
inferred← citeshttps://doi.org/10.1002/9783527618248.ch36openalex-snapshot
Redox Enzymes: Correlation of Three‐Dimensional Structure and Mechanism for Heme‐Containing Oxygenases and Peroxidases
inferred← citeshttps://doi.org/10.1002/9783527619450.ch9openalex-snapshot
C‐H Transformation at Unfunctionalized Alkanes
inferred← citeshttps://doi.org/10.1002/9783527622481.ch2openalex-snapshot
Directed Evolution as a Means to Engineer Enantioselective Enzymes
inferred← citeshttps://doi.org/10.1002/9783527623273.ch2openalex-snapshot
Iron Catalysis in Biological and Biomimetic Reactions
inferred← citeshttps://doi.org/10.1002/9783527625468.ch18openalex-snapshot
Pentacoordinating Bis(oxazoline) Ligands with Secondary Binding Sites
inferred← citeshttps://doi.org/10.1002/9783527628698.hgc003openalex-snapshot
Chemistry and Applications of Iron– TAML Catalysts in Green Oxidation Processes Based on Hydrogen Peroxide
inferred← citeshttps://doi.org/10.1002/9783527628698.hgc025openalex-snapshot
Catalysis with Cytochrome P 450 Monooxygenases
inferred← citeshttps://doi.org/10.1002/9783527629213.ch3openalex-snapshot
Modeling Enzymatic Reactions in Metalloenzymes and Photobiology by Quantum Mechanics (QM) and Quantum Mechanics/Molecular Mechanics (QM/MM) Calculations
inferred← citeshttps://doi.org/10.1002/9783527632039.ch12openalex-snapshot
Biooxidation with Cytochrome P450 Monooxygenases
inferred← citeshttps://doi.org/10.1002/9783527639861.ch30openalex-snapshot
Oxyfunctionalization of CH Bonds
inferred← citeshttps://doi.org/10.1002/9783527639861.ch31openalex-snapshot
Oxyfunctionalization of CC Multiple Bonds
inferred← citeshttps://doi.org/10.1002/9783527673261.ch06openalex-snapshot
QM/MM Studies of Structure and Reactivity of Cytochrome P450 Enzymes: Methodology and Selected Applications
inferred← citeshttps://doi.org/10.1002/9783527682492.ch5openalex-snapshot
Multi‐Enzyme Systems and Cascade Reactions Involving Cytochrome P450 Monooxygenases
inferred← citeshttps://doi.org/10.1002/9783527815128.ch9openalex-snapshot
Engineered Cytochromes P 450 for Biocatalysis
inferred← citeshttps://doi.org/10.1002/9783527834242.chf0223openalex-snapshot
High‐Valent Oxomanganese Complexes of Relevance in Oxyfunctionalization of Hydrocarbons
inferred← citeshttps://doi.org/10.1002/9783527834242.chf0230openalex-snapshot
Iron Catalyzed CH Amination
inferred← citeshttps://doi.org/10.1002/9783527834242.chf0239openalex-snapshot
Iron‐Catalyzed CH Bond Hydroxylation
inferred← citeshttps://doi.org/10.1002/adsc.200303049openalex-snapshot
Metal‐Free, Selective Alkane Functionalizations
inferred← citeshttps://doi.org/10.1002/adsc.201300716openalex-snapshot
Biomimetic Iron‐Catalyzed Asymmetric Epoxidations: Fundamental Concepts, Challenges and Opportunities
inferred← citeshttps://doi.org/10.1002/adsc.201300882openalex-snapshot
Oxidative Alkene Cleavage by Chemical and Enzymatic Methods
inferred← citeshttps://doi.org/10.1002/adsc.202301453openalex-snapshot
Acid‐Cooperative Transition Metal‐Catalysed Oxygen‐Atom‐Transfer: Ruthenium‐Catalysed C−H Oxygenation
inferred← citeshttps://doi.org/10.1002/ange.1874384openalex-snapshot
Janus Reactivity of a Mononuclear Non‐Heme Iron(III)‐Peroxo Complex Toward Indole Oxidation
inferred← citeshttps://doi.org/10.1002/ange.200300578openalex-snapshot
Die Rolle von Radikalen bei metallvermittelten Oxygenierungen
inferred← citeshttps://doi.org/10.1002/ange.200351415openalex-snapshot
Isolation and Crystal Structure of a Peroxo‐Bridged Heme–Copper Complex
inferred← citeshttps://doi.org/10.1002/ange.200351694openalex-snapshot
A Dramatic Push Effect on the Homolysis of FeIII(OOR) Intermediates To Form Non‐Heme FeIVO Complexes
inferred← citeshttps://doi.org/10.1002/ange.200352943openalex-snapshot
Porphyrin Traps Its Terminator! Concerted and Stepwise Porphyrin Degradation Mechanisms Induced by Heme‐Oxygenase and Cytochrome P450
inferred← citeshttps://doi.org/10.1002/ange.200353338openalex-snapshot
Biokatalytische asymmetrische Epoxidierung kombiniert mit NADH‐Regenerierung in organisch‐wässrigen Emulsionen
inferred← citeshttps://doi.org/10.1002/ange.200390004openalex-snapshot
Reversible Formation of Iodosylbenzene–Iron Porphyrin Intermediates in the Reaction of Oxoiron( IV ) Porphyrin π‐Cation Radicals and Iodobenzene
inferred← citeshttps://doi.org/10.1002/ange.200461527openalex-snapshot
Spin‐State Rationale for the Peroxo‐Stabilizing Role of the Thiolate Ligand in Superoxide Reductase
inferred← citeshttps://doi.org/10.1002/ange.200462182openalex-snapshot
Comparison of FeIVO Heme and Non‐heme Species: Electronic Structures, Bonding, and Reactivities
inferred← citeshttps://doi.org/10.1002/ange.200500623openalex-snapshot
Mechanistic Insight into Alcohol Oxidation by High‐Valent Iron–Oxo Complexes of Heme and Nonheme Ligands
inferred← citeshttps://doi.org/10.1002/ange.200501615openalex-snapshot
Rhodiumvermittelte Bildung von Peroxiden aus Disauerstoff: Isolierung von Hydroperoxo‐, Silylperoxo‐ und Methylperoxo‐Intermediaten
inferred← citeshttps://doi.org/10.1002/ange.200601574openalex-snapshot
Biokatalytische einstufige Alkenspaltung von Arylalkenen: ein enzymatisches Äquivalent zur reduktiven Ozonisierung
inferred← citeshttps://doi.org/10.1002/ange.200601927openalex-snapshot
Coordination‐Number Dependence of Reactivity in an Imidoiron(III) Complex
inferred← citeshttps://doi.org/10.1002/ange.200603060openalex-snapshot
Regio‐ and Chemoselective Enzymatic N‐Oxygenation In Vivo, In Vitro, and in Flow
inferred← citeshttps://doi.org/10.1002/ange.200603139openalex-snapshot
Inverse Axial‐Ligand Effects in the Activation of H2O2 and ROOH by an MnIII Corrolazine
inferred← citeshttps://doi.org/10.1002/ange.200605156openalex-snapshot
H2O2 Oxidations Catalyzed by an Iron(III) Corrolazine: Avoiding High‐Valent Iron–Oxido Species?
inferred← citeshttps://doi.org/10.1002/ange.200700068openalex-snapshot
Hydrogen Peroxide Dependent Monooxygenations by Tricking the Substrate Recognition of Cytochrome P450BSβ
inferred← citeshttps://doi.org/10.1002/ange.200702616openalex-snapshot
Engineered Alkane‐Hydroxylating Cytochrome P450BM3 Exhibiting Nativelike Catalytic Properties
inferred← citeshttps://doi.org/10.1002/ange.200702867openalex-snapshot
Which Oxidant Is Really Responsible for Sulfur Oxidation by Cytochrome P450?
inferred← citeshttps://doi.org/10.1002/ange.200703089openalex-snapshot
A Binuclear Manganese Cluster That Catalyzes Radical‐Mediated N‐Oxygenation
inferred← citeshttps://doi.org/10.1002/ange.200704228openalex-snapshot
Contrasting cis and trans Effects on the Reactivity of Nonheme Oxoiron(IV) Complexes
inferred← citeshttps://doi.org/10.1002/ange.200800137openalex-snapshot
Extreme Rate Acceleration by Axial Thiolate Coordination on the Isomerization of Endoperoxide Catalyzed by Iron Porphyrin
inferred← citeshttps://doi.org/10.1002/ange.200800669openalex-snapshot
An Electron‐Transfer Series of High‐Valent Chromium Complexes with Redox Non‐Innocent, Non‐Heme Ligands
inferred← citeshttps://doi.org/10.1002/ange.200801832openalex-snapshot
Proton‐ and Reductant‐Assisted Dioxygen Activation by a Nonheme Iron(II) Complex to Form an Oxoiron(IV) Intermediate
inferred← citeshttps://doi.org/10.1002/ange.200906736openalex-snapshot
Ein biomimetisches Hydroperoxo‐Eisen(III)‐Porphyrin‐Intermediat
inferred← citeshttps://doi.org/10.1002/ange.201002733openalex-snapshot
A Low‐Spin Ruthenium(IV)–Oxo Complex: Does the Spin State Have an Impact on the Reactivity?
inferred← citeshttps://doi.org/10.1002/ange.201005597openalex-snapshot
A Regioselective Biocatalyst for Alkane Activation under Mild Conditions
inferred← citeshttps://doi.org/10.1002/ange.201100588openalex-snapshot
Distinct Reactivity Differences of Metal Oxo and Its Corresponding Hydroxo Moieties in Oxidations: Implications from a Manganese(IV) Complex Having Dihydroxide Ligand
inferred← citeshttps://doi.org/10.1002/ange.201102144openalex-snapshot
Conversion of Cobalt(II) Porphyrin into a Helical Cobalt(III) Complex of Acyclic Pentapyrrole
inferred← citeshttps://doi.org/10.1002/ange.201105266openalex-snapshot
Directing Protons to the Dioxygen Ligand of a Ruthenium(II) Complex with Pendent Amines in the Second Coordination Sphere
inferred← citeshttps://doi.org/10.1002/ange.201201848openalex-snapshot
Asymmetric Epoxidation of Conjugated Olefins with Dioxygen
inferred← citeshttps://doi.org/10.1002/ange.201203280openalex-snapshot
Katalytische, milde und selektive Oxyfunktionalisierung von linearen Alkanen: aktuelle Herausforderungen
inferred← citeshttps://doi.org/10.1002/ange.201300282openalex-snapshot
Highly Selective Hydroxylation of Benzene to Phenol by Wild‐type Cytochrome P450BM3 Assisted by Decoy Molecules
inferred← citeshttps://doi.org/10.1002/ange.201301487openalex-snapshot
Komplexe mit Stickstoffradikalliganden: Einteilung, spektroskopische Eigenschaften, Reaktivität und katalytische Anwendungen
inferred← citeshttps://doi.org/10.1002/ange.201305370openalex-snapshot
Comparison of the Reactivity of Nonheme Iron(IV)–Oxo versus Iron(IV)–Imido Complexes: Which is the Better Oxidant?
inferred← citeshttps://doi.org/10.1002/ange.201404272openalex-snapshot
Die Bedeutung von Metallionen für die mechanischen Eigenschaften von Biomaterialien auf Proteinbasis
inferred← citeshttps://doi.org/10.1002/ange.201407156openalex-snapshot
A cis‐Divacant Octahedral and Mononuclear Iron(IV) Imide
inferred← citeshttps://doi.org/10.1002/ange.201408462openalex-snapshot
Dioxygen Reactivity with a Ferrocene–Lewis Acid Pairing: Reduction to a Boron Peroxide in the Presence of Tris(pentafluorophenyl)borane
inferred← citeshttps://doi.org/10.1002/ange.201411995openalex-snapshot
Identification and Spectroscopic Characterization of Nonheme Iron(III) Hypochlorite Intermediates
inferred← citeshttps://doi.org/10.1002/ange.201502229openalex-snapshot
Olefin cis‐Dihydroxylation and Aliphatic CH Bond Oxygenation by a Dioxygen‐Derived Electrophilic Iron–Oxygen Oxidant
inferred← citeshttps://doi.org/10.1002/ange.201502367openalex-snapshot
Characterization of Mononuclear Non‐heme Iron(III)‐Superoxo Complex with a Five‐Azole Ligand Set
inferred← citeshttps://doi.org/10.1002/ange.201502925openalex-snapshot
Oxidative Decarboxylierung von kurzkettigen Fettsäuren zu 1‐Alkenen
inferred← citeshttps://doi.org/10.1002/ange.201610129openalex-snapshot
Biokatalyse mit nicht‐natürlichen Aminosäuren: Enzymologie trifft Xenobiologie
inferred← citeshttps://doi.org/10.1002/ange.201705322openalex-snapshot
Total Synthesis of (−)‐N‐Methylwelwitindolinone B Isothiocyanate
inferred← citeshttps://doi.org/10.1002/ange.201710370openalex-snapshot
Conversion of Olefins into Ketones by an Iron‐Catalyzed Wacker‐type Oxidation Using Oxygen as the Sole Oxidant
inferred← citeshttps://doi.org/10.1002/ange.201901608openalex-snapshot
Direct Observation of Primary C−H Bond Oxidation by an Oxido‐Iron(IV) Porphyrin π‐Radical Cation Complex in a Fluorinated Carbon Solvent
inferred← citeshttps://doi.org/10.1002/ange.201916592openalex-snapshot
Oriented (Local) Electric Fields Drive the Millionfold Enhancement of the H‐Abstraction Catalysis Observed for Synthetic Metalloenzyme Analogues
inferred← citeshttps://doi.org/10.1002/ange.202002364openalex-snapshot
Synthesis of a “Masked” Terminal Zinc Sulfide and Its Reactivity with Brønsted and Lewis Acids
inferred← citeshttps://doi.org/10.1002/ange.202005554openalex-snapshot
In Vitro Reconstitution Reveals a Central Role for the N‐Oxygenase PvfB in (Dihydro)pyrazine‐N‐oxide and Valdiazen Biosynthesis
inferred← citeshttps://doi.org/10.1002/ange.202013791openalex-snapshot
Ferric Heme Superoxide Reductive Transformations to Ferric Heme (Hydro)Peroxide Species: Spectroscopic Characterization and Thermodynamic Implications for H‐Atom Transfer (HAT)
inferred← citeshttps://doi.org/10.1002/ange.202102484openalex-snapshot
Effect of the Ligand Backbone on the Reactivity and Mechanistic Paradigm of Non‐Heme Iron(IV)‐Oxo during Olefin Epoxidation
inferred← citeshttps://doi.org/10.1002/ange.202103222openalex-snapshot
Iron‐Catalyzed Wacker‐type Oxidation of Olefins at Room Temperature with 1,3‐Diketones or Neocuproine as Ligands**
inferred← citeshttps://doi.org/10.1002/ange.202114048openalex-snapshot
Electrochemical Trifluoromethoxylation of (Hetero)aromatics with a Trifluoromethyl Source and Oxygen
inferred← citeshttps://doi.org/10.1002/ange.202211521openalex-snapshot
The Role of Heme Peroxo Oxidants in the Rational Mechanistic Modeling of Nitric Oxide Synthase: Characterization of Key Intermediates and Elucidation of the Mechanism
inferred← citeshttps://doi.org/10.1002/ange.202310785openalex-snapshot
Insights into Cytochrome P450 Enzyme Catalyzed Defluorination of Aromatic Fluorides
inferred← citeshttps://doi.org/10.1002/ange.202409430openalex-snapshot
A Cytochrome P450 TxtE Model System with Mechanistic and Theoretical Evidence for a Heme Peroxynitrite Active Species
inferred← citeshttps://doi.org/10.1002/ange.202512839openalex-snapshot
Mechanistic Divergence in Sulfur‐Ligated Iron(III)‐Alkylperoxo Reactivity: Aldehyde Oxidation Prevails over Deformylation
inferred← citeshttps://doi.org/10.1002/ange.202517464openalex-snapshot
Are Atomic‐Oxygen‐Like Intermediates the Key to Metal–Oxo Catalyzed O–O Bond Formation?
inferred← citeshttps://doi.org/10.1002/ange.202522019openalex-snapshot
Heme Peroxo Reaction Intermediates: Mimicking Biological Structure and Reactivity With Synthetic Model Systems
inferred← citeshttps://doi.org/10.1002/ange.7072895openalex-snapshot
Distinct Oxidoreductases Orchestrate Indolethiophene Skeleton Formation and N ‐Hydroxylation‐Mediated Bioactivation in Thienoxidolin Biosynthesis
inferred← citeshttps://doi.org/10.1002/anie.1874384openalex-snapshot
Janus Reactivity of a Mononuclear Non‐Heme Iron(III)‐Peroxo Complex Toward Indole Oxidation
inferred← citeshttps://doi.org/10.1002/anie.200300578openalex-snapshot
The Role of Radicals in Metal‐Assisted Oxygenation Reactions
inferred← citeshttps://doi.org/10.1002/anie.200351415openalex-snapshot
Isolation and Crystal Structure of a Peroxo‐Bridged Heme–Copper Complex
inferred← citeshttps://doi.org/10.1002/anie.200351694openalex-snapshot
A Dramatic Push Effect on the Homolysis of FeIII(OOR) Intermediates To Form Non‐Heme FeIVO Complexes
inferred← citeshttps://doi.org/10.1002/anie.200352943openalex-snapshot
Porphyrin Traps Its Terminator! Concerted and Stepwise Porphyrin Degradation Mechanisms Induced by Heme‐Oxygenase and Cytochrome P450
inferred← citeshttps://doi.org/10.1002/anie.200353338openalex-snapshot
Coupling of Biocatalytic Asymmetric Epoxidation with NADH Regeneration in Organic–Aqueous Emulsions
inferred← citeshttps://doi.org/10.1002/anie.200390036openalex-snapshot
Reversible Formation of Iodosylbenzene–Iron Porphyrin Intermediates in the Reaction of Oxoiron( IV ) Porphyrin π‐Cation Radicals and Iodobenzene
inferred← citeshttps://doi.org/10.1002/anie.200461527openalex-snapshot
Spin‐State Rationale for the Peroxo‐Stabilizing Role of the Thiolate Ligand in Superoxide Reductase
inferred← citeshttps://doi.org/10.1002/anie.200462182openalex-snapshot
Comparison of FeIVO Heme and Non‐heme Species: Electronic Structures, Bonding, and Reactivities
inferred← citeshttps://doi.org/10.1002/anie.200500623openalex-snapshot
Mechanistic Insight into Alcohol Oxidation by High‐Valent Iron–Oxo Complexes of Heme and Nonheme Ligands
inferred← citeshttps://doi.org/10.1002/anie.200501615openalex-snapshot
Rhodium‐Mediated Formation of Peroxides from Dioxygen: Isolation of Hydroperoxo, Silylperoxo, and Methylperoxo Intermediates
inferred← citeshttps://doi.org/10.1002/anie.200601574openalex-snapshot
Biocatalytic Single‐Step Alkene Cleavage from Aryl Alkenes: An Enzymatic Equivalent to Reductive Ozonization
inferred← citeshttps://doi.org/10.1002/anie.200601927openalex-snapshot
Coordination‐Number Dependence of Reactivity in an Imidoiron(III) Complex
inferred← citeshttps://doi.org/10.1002/anie.200603060openalex-snapshot
Regio‐ and Chemoselective Enzymatic N‐Oxygenation In Vivo, In Vitro, and in Flow
inferred← citeshttps://doi.org/10.1002/anie.200603139openalex-snapshot
Inverse Axial‐Ligand Effects in the Activation of H2O2 and ROOH by an MnIII Corrolazine
inferred← citeshttps://doi.org/10.1002/anie.200605156openalex-snapshot
H2O2 Oxidations Catalyzed by an Iron(III) Corrolazine: Avoiding High‐Valent Iron–Oxido Species?
inferred← citeshttps://doi.org/10.1002/anie.200700068openalex-snapshot
Hydrogen Peroxide Dependent Monooxygenations by Tricking the Substrate Recognition of Cytochrome P450BSβ
inferred← citeshttps://doi.org/10.1002/anie.200702616openalex-snapshot
Engineered Alkane‐Hydroxylating Cytochrome P450BM3 Exhibiting Nativelike Catalytic Properties
inferred← citeshttps://doi.org/10.1002/anie.200702867openalex-snapshot
Which Oxidant Is Really Responsible for Sulfur Oxidation by Cytochrome P450?
inferred← citeshttps://doi.org/10.1002/anie.200703089openalex-snapshot
A Binuclear Manganese Cluster That Catalyzes Radical‐Mediated N‐Oxygenation
inferred← citeshttps://doi.org/10.1002/anie.200704228openalex-snapshot
Contrasting cis and trans Effects on the Reactivity of Nonheme Oxoiron(IV) Complexes
inferred← citeshttps://doi.org/10.1002/anie.200800137openalex-snapshot
Extreme Rate Acceleration by Axial Thiolate Coordination on the Isomerization of Endoperoxide Catalyzed by Iron Porphyrin
inferred← citeshttps://doi.org/10.1002/anie.200800669openalex-snapshot
An Electron‐Transfer Series of High‐Valent Chromium Complexes with Redox Non‐Innocent, Non‐Heme Ligands
inferred← citeshttps://doi.org/10.1002/anie.200801832openalex-snapshot
Proton‐ and Reductant‐Assisted Dioxygen Activation by a Nonheme Iron(II) Complex to Form an Oxoiron(IV) Intermediate
inferred← citeshttps://doi.org/10.1002/anie.200906736openalex-snapshot
A Biomimetic Ferric Hydroperoxo Porphyrin Intermediate
inferred← citeshttps://doi.org/10.1002/anie.201002733openalex-snapshot
A Low‐Spin Ruthenium(IV)–Oxo Complex: Does the Spin State Have an Impact on the Reactivity?
inferred← citeshttps://doi.org/10.1002/anie.201005597openalex-snapshot
A Regioselective Biocatalyst for Alkane Activation under Mild Conditions
inferred← citeshttps://doi.org/10.1002/anie.201100588openalex-snapshot
Distinct Reactivity Differences of Metal Oxo and Its Corresponding Hydroxo Moieties in Oxidations: Implications from a Manganese(IV) Complex Having Dihydroxide Ligand
inferred← citeshttps://doi.org/10.1002/anie.201102144openalex-snapshot
Conversion of Cobalt(II) Porphyrin into a Helical Cobalt(III) Complex of Acyclic Pentapyrrole
inferred← citeshttps://doi.org/10.1002/anie.201105266openalex-snapshot
Directing Protons to the Dioxygen Ligand of a Ruthenium(II) Complex with Pendent Amines in the Second Coordination Sphere
inferred← citeshttps://doi.org/10.1002/anie.201201848openalex-snapshot
Asymmetric Epoxidation of Conjugated Olefins with Dioxygen
inferred← citeshttps://doi.org/10.1002/anie.201203280openalex-snapshot
Catalytic, Mild, and Selective Oxyfunctionalization of Linear Alkanes: Current Challenges
inferred← citeshttps://doi.org/10.1002/anie.201300282openalex-snapshot
Highly Selective Hydroxylation of Benzene to Phenol by Wild‐type Cytochrome P450BM3 Assisted by Decoy Molecules
inferred← citeshttps://doi.org/10.1002/anie.201301487openalex-snapshot
Complexes with Nitrogen‐Centered Radical Ligands: Classification, Spectroscopic Features, Reactivity, and Catalytic Applications
inferred← citeshttps://doi.org/10.1002/anie.201305370openalex-snapshot
Comparison of the Reactivity of Nonheme Iron(IV)–Oxo versus Iron(IV)–Imido Complexes: Which is the Better Oxidant?
inferred← citeshttps://doi.org/10.1002/anie.201404272openalex-snapshot
The Mechanical Role of Metal Ions in Biogenic Protein‐Based Materials
inferred← citeshttps://doi.org/10.1002/anie.201407156openalex-snapshot
A cis ‐Divacant Octahedral and Mononuclear Iron(IV) Imide
inferred← citeshttps://doi.org/10.1002/anie.201408462openalex-snapshot
Dioxygen Reactivity with a Ferrocene–Lewis Acid Pairing: Reduction to a Boron Peroxide in the Presence of Tris(pentafluorophenyl)borane
inferred← citeshttps://doi.org/10.1002/anie.201411995openalex-snapshot
Identification and Spectroscopic Characterization of Nonheme Iron(III) Hypochlorite Intermediates
inferred← citeshttps://doi.org/10.1002/anie.201502229openalex-snapshot
Olefin cis‐Dihydroxylation and Aliphatic CH Bond Oxygenation by a Dioxygen‐Derived Electrophilic Iron–Oxygen Oxidant
inferred← citeshttps://doi.org/10.1002/anie.201502367openalex-snapshot
Characterization of Mononuclear Non‐heme Iron(III)‐Superoxo Complex with a Five‐Azole Ligand Set
inferred← citeshttps://doi.org/10.1002/anie.201502925openalex-snapshot
Oxidative Decarboxylation of Short‐Chain Fatty Acids to 1‐Alkenes
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