Nanoisozymes : The Origin behind Pristine CeO2 as Enzyme‐mimetics

Research output: Journal Publications and ReviewsRGC 21 - Publication in refereed journalpeer-review

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Original languageEnglish
Pages (from-to)10598-10606
Journal / PublicationChemistry - A European Journal
Issue number46
Online published4 Jun 2020
Publication statusPublished - 17 Aug 2020


It is well‐known that the interplay between molecules and active sites on the topmost surface of solid catalyst determines its activity in heterogeneous catalysis. The electron density of active site is believed to affect both adsorption and activation of reactant molecules at surface. Unfortunately, commercial X‐ray photoelectron spectroscopy (XPS) often adopted for such characterization is not sensitive enough to catalyst’ topmost surface. In our opinion, most researchers fail to acknowledge this point during their catalytic correlation, leading to different interpretations found in literatures over the past decades. Recent studies on pristine Cu2O (Nat. Catal. 2019, 2, 889; Nat. Energy 2019, 4, 957) have clearly suggested that the electron density of surface Cu is facet dependent and plays a key role in CO2 reduction. Herein, we show that pristine CeO2 can reach 2506%/1133% increase in phosphatase‐/peroxidase‐like activity once the exposed surface is wisely selected. Using nuclear magnetic resonance (NMR) with surface probe, the electron density of surface Ce (i.e. the active site) is found facet‐dependent and the key factor dictating their enzyme mimicking activities. Most importantly, the surface area of those CeO2 morphologies was demonstrated to become a factor only when their surface Ce can activate the adsorbed reactant molecules.

Research Area(s)

  • Nanoisozyme, Ceria, Facet-dependent electron density, Enzyme-like activity