Copper–oxygen adducts: new trends in characterization and properties towards C–H activation

De Tovar, Jonathan; Leblay, Rébecca; Wang, Yongxing; Wojcik, Laurianne; Thibon-Pourret, Aurore; Réglier, Marius; Simaan, A. Jalila; Le Poul, Nicolas; Belle, Catherine

doi:10.1039/d4sc01762e

Chem. Sci.

2024

DOI: 10.1039/d4sc01762e

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Copper–oxygen adducts: new trends in characterization and properties towards C–H activation

Jonathan De Tovar,

Rébecca Leblay,

Yongxing Wang

et al.

Abstract: This review summarizes the latest discoveries in the field of C−H activation by copper monoxygenases and more particularly by their bioinspired systems. This work first describes recent background on copper-containing...

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Cited by 6 publications

References 305 publications

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Structural Snapshots, Trajectory and Thermodynamics of the Reversible μ‐1,2‐Peroxo/μ‐1,1‐Hydroperoxo Dicopper(II) Interconversion

Spyra,

Hiller,

Eisenlohr

et al. 2024

Angewandte Chemie

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Hydrogen bonds involving the oxygen atoms of intermediates that result from copper‐mediated O2 activation play a key role for controlling the reactivity of Cux/O2 active sites in metalloenzymes and synthetic model complexes. However, structural insight into H‐bonding in such transient species as well as thermodynamic information about proton transfer to or from the O2‐derived ligands is scarce. Here we present a detailed study of the reversible interconversion of a μ1,2‐peroxodicopper(II) complex ([1]+) and its μ1,1‐hydroperoxo congener ([2]+) via (de)protonation, including the isolation and structural characterization of several H‐bond donor (HBD) adducts of [1]+ and the determination of binding constants. For one of these adducts a temperature‐dependent μ1,2‐peroxo/μ1,1‐hydroperoxo equilibrium associated with reversible H+‐translocation is observed, its thermodynamics investigated experimentally and computationally, and effects of H‐bonding on spectroscopic parameters of the CuII2(μ1,2‐O2) species are revealed. DFT calculations allowed to fully map and correlate the trajectories of H+‐transfer and μ1,2‐peroxo→μ1,1‐peroxo rearrangement. These findings enhance our understanding of two key intermediates in bioinspired Cu2/O2 chemistry.

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Structural Snapshots, Trajectory and Thermodynamics of the Reversible μ‐1,2‐Peroxo/μ‐1,1‐Hydroperoxo Dicopper(II) Interconversion

Spyra,

Hiller,

Eisenlohr

et al. 2024

Angewandte Chemie

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show abstract

Structural Snapshots, Trajectory and Thermodynamics of the Reversible μ‐1,2‐Peroxo/μ‐1,1‐Hydroperoxo Dicopper(II) Interconversion

Spyra,

Hiller,

Eisenlohr

et al. 2024

Angew Chem Int Ed

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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

Panda,

Phan,

Dunietz

et al. 2024

J. Am. Chem. Soc.

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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.

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Copper–oxygen adducts: new trends in characterization and properties towards C–H activation

Abstract: This review summarizes the latest discoveries in the field of C−H activation by copper monoxygenases and more particularly by their bioinspired systems. This work first describes recent background on copper-containing...

Cited by 6 publications

References 305 publications

Structural Snapshots, Trajectory and Thermodynamics of the Reversible μ‐1,2‐Peroxo/μ‐1,1‐Hydroperoxo Dicopper(II) Interconversion

Structural Snapshots, Trajectory and Thermodynamics of the Reversible μ‐1,2‐Peroxo/μ‐1,1‐Hydroperoxo Dicopper(II) Interconversion

Structural Snapshots, Trajectory and Thermodynamics of the Reversible μ‐1,2‐Peroxo/μ‐1,1‐Hydroperoxo Dicopper(II) Interconversion

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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Copper–oxygen adducts: new trends in characterization and properties towards C–H activation

Abstract: This review summarizes the latest discoveries in the field of C−H activation by copper monoxygenases and more particularly by their bioinspired systems. This work first describes recent background on copper-containing...

Cited by 6 publications

References 305 publications

Structural Snapshots, Trajectory and Thermodynamics of the Reversible μ‐1,2‐Peroxo/μ‐1,1‐Hydroperoxo Dicopper(II) Interconversion

Structural Snapshots, Trajectory and Thermodynamics of the Reversible μ‐1,2‐Peroxo/μ‐1,1‐Hydroperoxo Dicopper(II) Interconversion

Structural Snapshots, Trajectory and Thermodynamics of the Reversible μ‐1,2‐Peroxo/μ‐1,1‐Hydroperoxo Dicopper(II) Interconversion

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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Product

Resources

About

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