Emergence of a Promiscuous Peroxidase Under Non‐Equilibrium Conditions**

Abstract

Herein, we report the substrate induced generation of a transient catalytic microenvironment from a single amino acid functionalized fatty acid in presence of a cofactor hemin. The catalytic state accessed under non-equilibrium conditions showed acceleration of peroxidase activity resulting in degradation of the substrate and subsequently led to disassembly. Equilibrated systems could not access the three-dimensional microphases and showed substantially lower catalytic activity. Further, the assembled state showed latent catalytic function (promiscuity) to hydrolyze a precursor to yield the same substrate. Consequently, the assembly demonstrated protometabolism by exploiting the peroxidase-hydrolase cascade to augment the lifetime and the mechanical properties of the catalytic state.

Systems chemistry of peptide-assemblies for biochemical transformations

“…Recently, the same group used peroxidase activity under an oxidizing environment to develop such non-equilibrium transient catalytic assemblies. 186 In this context, the amphiphile C18H was used which in the presence of cofactor hemin and substrate (X) induced the generation of the three-dimensional catalytic networks (S1, Fig. 11d).…”

Transient Biomacromolecular Nanoparticles for Labels with Self‐Erasable and Rewritable Ability

“…[45] Despite the progress in the field, the number of synthetic molecules for chemical fueldriven non-equilibrium self-assembly systems remains rather limited. [46][47][48][49][50] There were also some limitations in the synthesis of molecules for non-equilibrium self-assembly, including costand labor-consuming preparation, toxicity, and the difficulty to mass-produce. In comparison with synthetic molecules, natural polymers have the advantages of low cost, low toxicity, and sustainability.…”

Temporally Controlled Multienzyme Catalysis Using a Dissipative Supramolecular Nanozyme

“…Life is powered by multienzymatic tandem reactions with unprecedented catalytic efficiencies, owing to unique aspects of biological reactors such as compartmentalization, nanoconfinement, and out-of-equilibrium dynamics. , However, the majority of known nanozymes to date operates in an “always-on” mode, − despite the catalytic processes in the biological systems being far away from equilibrium. , Efforts have been made to mimic the nonequilibrium catalytic property through fuel-mediated self-assembled systems with temporally regulated catalytic properties. , Various fuels such as pH, temperature, light, and chemical moieties have been utilized in driving the self-assembly of supramolecular ensembles to generate transient self-assembled nanostructures. ,− However, transient self-assembled systems with multienzymatic activities such as laccase and peroxidases in a dynamic out-of-equilibrium system are lacking . Herein, we present a supramolecular strategy for the autonomous generation of a nanozyme with multienzymatic activity, temporally controlled by a fuel.…”

“…38,39 Efforts have been made to mimic the nonequilibrium catalytic property through fuel-mediated self-assembled systems with temporally regulated catalytic properties. 40,41 Various fuels such as pH, temperature, light, and chemical moieties have been utilized in driving the self-assembly of supramolecular ensembles to generate transient self-assembled nanostructures. 33,41−43 However, transient self-assembled systems with multienzymatic activities such as laccase and peroxidases in a dynamic out-ofequilibrium system are lacking.…”