The cooperativity and nonlinear dynamics are among the many fundamental characteristics of life. Many molecular mechanisms, such as haemoglobin oxygen binding, actin polymerisation, microtubule dynamic assembly, and Ca2+ ion channels, are assembly-coupled cooperative phenomena in living systems. Natural enzymes are one such systems that rely heavily on the supramolecular environment and non-covalent interactions for their function. However, natural enzymes, their tuning, and their application under robust conditions are complex and challenging. Still, only a limited number of examples exist where minimal assemblies are coupled to enzyme-like functions. Inspired by such principles, we investigate enzyme-like catalysis in copper-tyrosine self-assembled networks (CuY SANs) as a model system for coordination-driven nonlinear catalytic regulation.
The structural organisation of CuY SANs is comprehensively characterised, revealing the formation of well-defined supramolecular nanoassemblies in both the solid and solution
phases. Finally, the Michaelis-Menten parameters and the nonlinear dynamics are studied using the o-phenylenediamine oxidation reaction, demonstrating peroxidase-like catalytic activity. Finally, the ordered assembly formation of CuY SANs and their EDTA-dependent reorganisation leading to a non-linear effect in catalysis was simulated using molecular dynamics. Notably, this study reports the first example of a single tyrosine coordinated to copper, forming a self-assembled nanozyme. Enzyme-like regulation, supramolecular assembly, and nonlinear coordination-driven masking of catalytic activity are the unique features of the CuY self-assembled nanozyme. Further, the enzyme-like activity emerging from minimal non-proteinaceous metal-ligand complexes represents a critical prebiotic bridge between inanimate matter and living chemical networks. Therefore, the present study opens avenues for understanding and generating minimalist enzyme-like assemblies that exhibit characteristic life-like features
