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

Synthetic side-on peroxide-bound dicopper­(II) ( S P) complexes are important for understanding the active site structure/function of many copper-containing enzymes. This work highlights the formation of new {CuII(μ-η2:η2-O2 2–)­CuII} complexes (with electronic absorption and resonance Raman (rR) sp...

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Veröffentlicht in:Journal of the American Chemical Society 2024-06, Vol.146 (22), p.14942-14947
Hauptverfasser: Panda, Sanjib, Phan, Hai, Dunietz, Eleanor M., Brueggemeyer, Magdalene T., Hota, Pradip Kumar, Siegler, Maxime A., Jose, Anex, Bhadra, Mayukh, Solomon, Edward I., Karlin, Kenneth D.
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container_end_page 14947
container_issue 22
container_start_page 14942
container_title Journal of the American Chemical Society
container_volume 146
creator Panda, Sanjib
Phan, Hai
Dunietz, Eleanor M.
Brueggemeyer, Magdalene T.
Hota, Pradip Kumar
Siegler, Maxime A.
Jose, Anex
Bhadra, Mayukh
Solomon, Edward I.
Karlin, Kenneth D.
description Synthetic side-on peroxide-bound dicopper­(II) ( S P) complexes are important for understanding the active site structure/function of many copper-containing enzymes. This work highlights the formation of new {CuII(μ-η2:η2-O2 2–)­CuII} 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 ligand para-CC coupling. The newly observed chemistry in these ligand–Cu systems is discussed with respect to (a) our Cu-MeAN (tridentate N,N,N′,N′,N″-pentamethyl­dipropylenetriamine)-derived model S P species, which was unreactive toward exogenous monophenol addition (J. Am. Chem. Soc. 2012, 134, 8513–8524), emphasizing the impact of intramolecularly tethered ArOH groups, and (b) recent advances in understanding the mechanism of action of the tyrosinase (Ty) enzyme.
doi_str_mv 10.1021/jacs.4c04402
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source American Chemical Society Journals
subjects absorption
active sites
enzymes
ligands
mechanism of action
species
spectral analysis
spectroscopy
title 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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