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Structural and Functional Investigations on Diiron Complexes: Catalase‐Like Activity and Mechanistic Studies on the Formation of (μ‐Peroxo)diiron(III) Adducts

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This article is published in European Journal of Inorganic Chemistry.The article was published on 1999-09-01. It has received 17 citations till now.

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Mononuclear non-heme iron(III) peroxide complexes: syntheses, characterisation, mass spectrometric and kinetic studies

TL;DR: In this article, a series of transient interconvertible protonated and deprotonated mononuclear Fe(III) peroxo species were derived from the pH dependent reaction of dihydrogen peroxide with either iron (II) or iron (III) complexes of general formulation [Fe(Rtpen)X](A)n, n======= 1, 2; X = Cl, Br; Rtpen =======N-alkyl-N,N′, N′-tris(2-pyridylmethyl)ethane
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Synthesis, Structure, and Catalytic Activity of New μ‐Oxo‐Bridged Diiron(III) Complexes

TL;DR: In this article, the preparation and characterisation of two dinuclear iron(III) complexes with tripodal ligands 1,3-bis(2′-pyridylimino)isoindoline (indH) are presented.
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Heterodinuclear zinc(II)-iron(III) complexes and dinuclear zinc complexes as models for zinc-containing phosphatases

TL;DR: In this article, five dinuclear model complexes for zinc-containing phosphatases with dinucleating ligands have been prepared and characterized by single-crystal X-ray crystallography.
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Methane monooxygenase and its related biomimetic models.

TL;DR: Recent spectroscopic and structural studies on various biomimetic model compounds have provided new and valuable insights into methane monooxygenase's mechanism of action and the important dioxygen-activation process.
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Rapid phosphorus triester hydrolysis catalyzed by bimetallic tetrabenzimidazole complexes

TL;DR: Bimetallic complexes based on the binucleating ligand N,N,N',N'-tetrakis and its new toluoyl ester derivative catalyze the hydrolysis of phosphorus triesters at ambient temperature with activities rivalling the fastest known systems.
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Three-dimensional structure of the free radical protein of ribonucleotide reductase

TL;DR: The enzyme ribonucleotide reductase furnishes precursors for the DNA synthesis of all living cells and one of its constituents, the free radical protein, has an unusual α-helical structure.
Journal ArticleDOI

Two-Metal Ion Catalysis in Enzymatic Acyl- and Phosphoryl-Transfer Reactions

TL;DR: A remarkable diversity is also seen in the structures of the active sites of these di- and trinuclear metalloenzymes, even for enzymes that catalyze very similar reactions, including hydrolytic cleavage of phosphomono-, -di- and -triester bonds, phosphoanhydride bonds as well as of peptide bonds or urea.
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