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Article
Oxidation of alkane and alkene moieties with biologically inspired nonheme iron catalysts and hydrogen peroxide: from free radicals to stereoselective transformations
The selective oxidation of hydrocarbons is a challenging reaction for synthetic chemists, but common in nature. Iron oxygenases activate the O–O bond of dioxygen to perform oxidation of alkane and alkenes moie...
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Article
Discussion of an open problem
Quantum mechanics rears its head in many places and one of them is inorganic chemistry, where the electronic spin associated with unpaired electrons has a profound influence. This was the topic of the 2012 CEC...
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Article
Observation of Fe(V)=O using variable-temperature mass spectrometry and its enzyme-like C–H and C=C oxidation reactions
Oxo-transfer chemistry mediated by iron underpins many biological processes and today is emerging as synthetically very important for the catalytic oxidation of C–H and C=C moieties that are hard to activate c...
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Article
Efficient water oxidation catalysts based on readily available iron coordination complexes
Water oxidation catalysis constitutes the bottleneck for the development of energy-conversion schemes based on sunlight. To date, state-of-the-art homogeneous water oxidation catalysis is performed efficiently...
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Article
Erratum to Oxoiron(IV) complexes of the tris(2-pyridylmethyl)amine ligand family: effect of pyridine α-substituents
Erratum to: J Biol Inorg Chem 11:272–276 DOI 10.1007/s00775-006-0089-6
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Article
Oxoiron(IV) complexes of the tris(2-pyridylmethyl)amine ligand family: effect of pyridine α-substituents
The oxoiron(IV) complexes of two 6-substituted tris(2-pyridylmethyl)amine ligand derivatives have been generated and characterized with respect to their spectroscopic and reactivity properties. The introductio...
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Article
4-Nitrocatechol as a probe of a Mn(II)-dependent extradiol-cleaving catechol dioxygenase (MndD): comparison with relevant Fe(II) and Mn(II) model complexes
Mn(II)-dependent 3,4-dihydroxyphenylacetate 2,3-dioxygenase (MndD) is an extradiol-cleaving catechol dioxygenase from Arthrobacter globiformis that has 82% sequence identity to and cleaves the same substrate (3,...
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Article
A nonheme iron(II) complex that models the redox cycle of lipoxygenase
The air-stable complex [Fe(6-Me3-TPA)(O2CAr)]+ [1; 6-Me3-TPA=tris(6-methyl-2-pyridylmethyl)amine] has been synthesized as a model for the iron(II) site of lipoxygenase. This iron(II) complex reacts with 0.5 equi...