Structural Analysis and Intrinsic Enzyme Mimicking Activities of Ligand‐Free PtAg Nanoalloys

Abstract Nanozymes are nanomaterials with biocatalytic properties under physiological conditions and are one class of artificial enzymes to overcome the high cost and low stability of natural enzymes. However, surface ligands on nanomaterials will decrease the catalytic activity of the nanozymes by blocking the active sites. To address this limitation, ligand‐free PtAg nanoclusters (NCs) are synthesized and applied as nanozymes for various enzyme‐mimicking reactions. By taking advantage of the mutual interaction of zeolitic imidazolate frameworks (ZIF‐8) and Pt precursors, a good dispersion of PtAg bimetal NCs with a diameter of 1.78 ± 0.1 nm is achieved with ZIF‐8 as a template. The incorporation of PtAgNCs in the voids of ZIF‐8 is confirmed with structural analysis using the atomic pair‐distribution function and powder X‐ray diffraction. Importantly, the PtAgNCs present good catalytic activity for various enzyme‐mimicking reactions, including peroxidase‐/catalase‐ and oxidase‐like reactions. Further, this work compares the catalytic activity between PtAg NCs and PtAg nanoparticles with different compositions and finds that these two nanozymes present a converse dependency of Ag‐loading on their activity. This study contributes to the field of nanozymes and presents a potential option to prepare ligand‐free bimetal biocatalysts with sizes in the nanocluster regime.