Chiral carbon dots (CDots) attract extensive attention
due to their
promising application in the biological field. Their biological effects
strongly depend on their chiral structure. Laccase (Lac) is a classic
multicopper-containing polyphenol oxidase. The impact of the chirality
of CDots on the Lac activity has not been fully emphasized and studied
yet. Here, chiral CDots are prepared by thermal polymerization from l/d-cysteine (l/d-Cys) and citric
acid (CA), where the obtained twins of chiral CDots possess all the
same properties such as size, charge, and elemental content, except
chirality. The d-CDots (256 μg mL–1) could improve the catalytic activity of Lac (88%), while the l-CDots have no obvious effect on Lac at the same concentration.
Based on the results of the Michaelis constant (K
m) and circular dichroism (CD) spectra, compared with l-CDots, the superior catalytic performance of d-CDots
is due to the preferable combination toward Lac, resulting in the
change of the α helix structure of Lac. Our work reveals the
important implications for solving the problem of limited and selective
regulation of enzyme activity.