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Substrate and Lewis Acid Coordination Promote O-O Bond Cleavage of an Unreactive L₂Cu^II₂(O₂^2-) Species to Form L₂Cu^III₂(O)₂ Cores with Enhanced Oxidative Reactivity.

ABSTRACT: Copper-dependent metalloenzymes are widespread throughout metabolic pathways, coupling the reduction of O₂ with the oxidation of organic substrates. Small-molecule synthetic analogs are useful platforms to generate L/Cu/O₂ species that reproduce the structural, spectroscopic, and reactive properties of some copper-/O₂-dependent enzymes. Landmark studies have shown that the conversion between dicopper(II)-peroxo species (L₂Cu^II₂(O₂^2-) either side-on peroxo, ^SP, or end-on trans-peroxo, ^TP) and dicopper(III)-bis(μ-oxo) (L₂Cu^III₂(O^2-)₂: O) can be controlled through ligand design, reaction conditions (temperature, solvent, and count

SUBMITTER: Garcia-Bosch I

PROVIDER: S-EPMC5532877 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

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Dataset Information

Substrate and Lewis Acid Coordination Promote O-O Bond Cleavage of an Unreactive L₂Cu^II₂(O₂^2-) Species to Form L₂Cu^III₂(O)₂ Cores with Enhanced Oxidative Reactivity.

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Substrate and Lewis Acid Coordination Promote O-O Bond Cleavage of an Unreactive L2CuII2(O22-) Species to Form L2CuIII2(O)2 Cores with Enhanced Oxidative Reactivity.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Substrate and Lewis Acid Coordination Promote O-O Bond Cleavage of an Unreactive L₂Cu^II₂(O₂^2-) Species to Form L₂Cu^III₂(O)₂ Cores with Enhanced Oxidative Reactivity.