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Hydroxylation of Phenolic Compounds by a Peroxodicopper(II) Complex: Further Insight into the Mechanism of Tyrosinase

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Outgoing claims: the papers this work cites, builds on, or argues with.

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Reversible Dioxygen Binding and Phenol Oxygenation in a Tyrosinase Model System

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Hemocyanin and tyrosinase models. Synthesis, azide binding, and electrochemistry of dinuclear copper(II) complexes with poly(benzimidazole) ligands modeling the met forms of the proteins

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Direct Conversion of Phenols to o-Quinones by Copper(I) Dioxygen. Questions Regarding the Monophenolase Activity of Tyrosinase Mimics

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Addition of fluorenylidene to 1,2-dichloroethylenes. Effects of additives and the question of spin-state equilibrium

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Three-coordinate binuclear copper(I) complex: model compound for the copper sites in deoxyhemocyanin and deoxytyrosinase

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A Stabilized μ-η2:η2 Peroxodicopper(II) Complex with a Secondary Diamine Ligand and Its Tyrosinase-like Reactivity

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Tyrosinase Reactivity in a Model Complex: An Alternative Hydroxylation Mechanism

inferredcites →https://doi.org/10.1201/9780203908457.ch14openalex-snapshot

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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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Copper-containing enzymes: Site types and low-molecular-weight model compounds

inferred← citeshttps://doi.org/10.3109/14756366.2013.782298openalex-snapshot

Indirect inactivation of tyrosinase in its action on 4- tert -butylphenol

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Non-Noble Metal Aromatic Oxidation Catalysis: From Metalloenzymes to Synthetic Complexes

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Fluorescent Bis(guanidine) Copper Complexes as Precursors for Hydroxylation Catalysis

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Asymmetric Sulfoxidation by a Tyrosinase Biomimetic Dicopper Complex with a Benzimidazolyl Derivative of L-Phenylalanine

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Complete σ* intramolecular aromatic hydroxylation mechanism through O2 activation by a Schiff base macrocyclic dicopper(I) complex

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Unique Functions of Metal Complexes Inspired by Control of Coordination Environment around Metal Ions

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