Abstract
Specificity and activity are often at odds for natural enzymes. In this work, specificity and activity in coronazymes made of an Au nanoparticle (AuNP) and coated with DNA aptamer for glucose substrates are decoupled. By single-molecule fluorescent MT-HILO (magnetic tweezers coupled with highly inclined and laminated optical sheet) microscopy, it is found that this coronazyme has ≈30 times higher activity on the d-glucose compared to bare AuNP nanozymes. Significantly, the new coronazyme demonstrates long-range modulations by circularly polarized light (CPL) according to the matching chirality between the CPL and DNA corona, which follows the rule of chiral induced spin selectivity (CISS). Although the aptamer in the coronazyme is evolved against d-glucose, surprisingly, this coronazyme catalyzes l-glucose better than d-glucose, likely due to the faster rates for the aptamer to interact with the l- over d-glucose. These results demonstrate, for the first time, an artificial enzyme with its catalytic activity controlled by short-range intermolecular forces, whereas its chiral specificity is modulated by long-range CPLs. This decoupled arrangement is pivotal to forge premier catalysts with activity and specificity superior to natural enzymes by separately optimizing these two properties.