Catalytic Activity of Copper Complexes in Biological Systems

Summary

Copper complexes have emerged as versatile catalysts in biological and biomimetic systems, owing to the metal’s accessible redox states and ability to coordinate a wide range of ligands. In nature, copper centres in enzymes such as tyrosinase and catechol oxidase facilitate the oxidation of phenolic substrates through controlled activation of molecular oxygen. Synthetic analogues mimic these activities by varying ligand denticity, donor atom identity and steric environment, thereby tuning redox potential, substrate specificity and reaction kinetics. Beyond oxidase models, copper complexes also serve as therapeutic agents, for instance by catalysing the production or scavenging of reactive oxygen species in cellular environments. Structural studies reveal that biomimetic copper centres can adopt mono-, di- or trinuclear geometries, each offering distinct mechanistic pathways for electron transfer and substrate binding. Advances in spectroscopic and electrochemical methods have allowed detailed characterisation of catalytic intermediates, shedding light on proton-coupled electron transfer processes critical to enzymatic turnover. The global significance of this field spans green oxidation processes, pharmaceutical development and biosensor technology, as copper-based catalysts offer earth-abundant and environmentally benign alternatives to noble metals. Current research aims to integrate these complexes into living systems, develop stimuli-responsive catalysts and harness photo-driven oxidation, thereby broadening applications in sustainable chemistry and medicine.

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Catalytic Activity of Copper Complexes in Biological Systems publication trend

The graph below shows the total number of articles in catalytic activity of copper complexes in biological systems across all publications each year (not limited to Nature Index journals).

Technical terms

Catecholase-like activity: The ability of a catalyst to oxidise catechols to o-quinones, mimicking natural catechol oxidase enzymes.

Turnover number (TON): The number of substrate molecules converted per catalyst molecule before deactivation.

Ligand denticity: The number of donor atoms within a ligand that coordinate to a metal centre.

Redox potential: The electrical potential at which a metal centre undergoes oxidation or reduction, influencing catalytic activity.

Proton-coupled electron transfer (PCET): A mechanistic pathway where proton and electron transfers occur simultaneously or in a concerted fashion, crucial in enzymatic redox reactions.

References

  1. Quinoline Derivatives with Different Functional Groups: Evaluation of Their Catecholase Activity. Catalysts (2022).
  2. Synthesis, Structure and Catechol Oxidase Activity of Mono Nuclear Cu(II) Complex with Phenol-Based Chelating Agent with N, N, O Donor Sites. Crystals (2022).
  3. New In Situ Catalysts Based on Nitro Functional Pyrazole Derivatives and Copper (II) Salts for Promoting Oxidation of Catechol to o-Quinone. Catalysts (2023).
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