A supramolecular metalloenzyme possessing robust oxidase-mimetic catalytic function

Area of Science:

• Biomimetic chemistry
• Supramolecular chemistry
• Catalysis

Background:

• Enzymes require specific 3D structures for function, but environmental changes can cause irreversible activity loss.
• Synthesizing enzyme-like active sites de novo is difficult due to challenges in replicating functional group spatial arrangements.

Purpose of the Study:

• To create a supramolecular mimetic enzyme using self-assembling nucleotides, fluorenylmethyloxycarbonyl (Fmoc)-modified amino acids, and copper.
• To investigate the catalytic functions and performance of this novel artificial catalyst compared to existing complexes.

Main Methods:

• Self-assembly of nucleotides with Fmoc-amino acids and copper to form a supramolecular structure.
• Experimental and theoretical analyses to understand the catalyst's structure-activity relationship.
• Evaluation of catalytic activity, focusing on oxidase-mimetic functions and thermal stability.

Main Results:

• The supramolecular catalyst mimics copper cluster-dependent oxidases with performance exceeding reported artificial complexes.
• Periodic arrangement of amino acids via fluorenyl stacking is crucial for forming oxidase-mimetic copper clusters.
• Nucleotides enhance copper activity by facilitating a copper-peroxide intermediate, enabling thermophilic behavior up to 95°C in water.

Conclusions:

• The developed supramolecular enzyme offers a promising platform for designing advanced biomimetic catalysts.
• Findings provide insights into the mechanisms of primordial redox enzymes.
• The catalyst's stability and efficiency highlight the potential of supramolecular approaches in artificial enzyme design.