Recently, a collaborative research team led by Professor Yong-Qiang Li of Shandong University and Professor Yanmei Yang of Shandong Normal University systematically investigated the physical binding mechanisms between enzymes and the photosensitizer chlorin e6 (Ce6), and proposed a catalytically enhanced strategy for photodynamic therapy (PDT). The study demonstrated that the extent of positively charged regions on the enzyme surface could be served as a reliable indicator for evaluating and predicting the enzyme’s binding affinity to Ce6. Based on this criterion, the authors further developed catalase-Ce6 nanoconjugates (CAT-Ce6 NCs) exhibiting excellent stability and potent photodynamic antibacterial activity. The CAT-Ce6 NCs effectively remodeled hypoxic pathological microenvironments and eradicated bacteria, thereby promoting the advancement of catalysis-augmented PDT of bacterial infections. The aforementioned study, titled "Deciphering the Physical Binding Mechanism of Enzyme–Photosensitizer Facilitates Catalysis-Augmented Photodynamic Therapy," was published in the journal Research.