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Intramolecular Phenolic H-Atom Abstraction by a N₃ArOH Ligand-Supported (μ-η²:η²-Peroxo)dicopper(II) Species Relevant to the Active Site Function of oxy-Tyrosinase.

ABSTRACT: Synthetic side-on peroxide-bound dicopper(II) (^SP) complexes are important for understanding the active site structure/function of many copper-containing enzymes. This work highlights the formation of new {Cu^II(μ-η²:η²-O₂^2-)Cu^II} complexes (with electronic absorption and resonance Raman (rR) spectroscopic characterization) using tripodal N₃ArOH ligands at -135 °C, which spontaneously participate in intramolecular phenolic H-atom abstraction (HAA). This results in the generation of bis(phenoxyl radical)bis(μ-OH)dicopper(II) intermediates, substantiated by their EPR/UV-vis/rR spectroscopic signatures and crystal structural determination of a diphenoquinone dicopper(I) complex derived from li

SUBMITTER: Panda S

PROVIDER: S-EPMC11193493 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature

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Dataset Information

Intramolecular Phenolic H-Atom Abstraction by a N₃ArOH Ligand-Supported (μ-η²:η²-Peroxo)dicopper(II) Species Relevant to the Active Site Function of oxy-Tyrosinase.

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Dataset Information

Intramolecular Phenolic H-Atom Abstraction by a N3ArOH Ligand-Supported (μ-η2:η2-Peroxo)dicopper(II) Species Relevant to the Active Site Function of oxy-Tyrosinase.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Intramolecular Phenolic H-Atom Abstraction by a N₃ArOH Ligand-Supported (μ-η²:η²-Peroxo)dicopper(II) Species Relevant to the Active Site Function of oxy-Tyrosinase.