【摘 要】
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Surface Lewis acid-base sites in crystal structure may influence the physicochemical properties and the catalytic performances in nanozymes.Understanding the synergistic effect mechanism of Co3O4 nanozymes towards substances (3,3\',5,5\'-tetramethylbe
【机 构】
：
Key Laboratory of Colloid and Interface Chemistry,Ministry of Education,School of Chemistry and Chem
论文部分内容阅读
Surface Lewis acid-base sites in crystal structure may influence the physicochemical properties and the catalytic performances in nanozymes.Understanding the synergistic effect mechanism of Co3O4 nanozymes towards substances (3,3\',5,5\'-tetramethylbenzidine(TMB) and hydrogen peroxide (H2O2)) induced by surface Lewis acid-base sites is important to enhance the efficiency for peroxidase-like reaction.Herein,ultrathin porous Co3O4 nanosheets with abundant Lewis acid-base sites were prepared by sodium borohydride (NaBH4) reduction treatment,which exhibited high-efficiency peroxidase-like activity compared with original Co3O4 nanosheets.The Lewis acid-base sites for ultrathin porous Co3O4 nanosheets nanozyme were owing to the coordination unsaturation of Co ions and the formation of defect structure.Ultrathin porous Co3O4 nanosheets had 18.26-fold higher catalytic efficiency (1.27 × 10-2 s-1·mM-1) than that of original Co3O4 (6.95 × 10-4 s-1·mM-1) in oxidizing TMB substrate.The synergistic effect of surface acid and base sites can enhance the interfacial electron transfer process of Co3O4 nanosheets,which can be a favor of absorption substrates and the generation of reactive intermediates such as radicals.Furthermore,the limit of detection of hydroquinol was 0.58 μM for ultrathin porous Co3O4 nanosheets,965-fold lower than original Co3O4 (560 μM).Besides,the linear range of ultrathin porous Co3O4 nanosheets was widely with the concentration of 5.0-1,000 μM.Colorimetric detection of hydroquinol by agarose-based hydrogel membrane was provided based on excellent peroxidase-like properties.This study provided insights into designing high-performance nanozymes for peroxidase-like catalysis via a strategy of solid surface acid-base sites engineering.
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