Regulating oxygen activation and catalytic kinetics in ZnCo2O4 nanozymes via Mn substitution: insights into the oxidase-like activity mechanism
Duong Hoang Thuc, Vu Thi Huong Mai, Chu Quynh Mai, Pham-Cong De, Van Tan Tran, Vinh Ya, Quoc Huy Thi, Xuan-Dinh Ngo, Van-Tuan Hoang, Anh-Tuan Le · 2026
Read Regulating oxygen activation and catalytic kinetics in ZnCo2O4 nanozymes via Mn substitution: insights into the oxidase-like activity mechanism by Duong Hoang Thuc, Vu Thi Huong Mai, Chu Quynh Mai, Pham-Cong De, Van Tan Tran, Vinh Ya, Quoc Huy Thi, Xuan-Dinh Ngo, Van-Tuan Hoang, Anh-Tuan Le (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13552416.txt.
Description
Duong Hoang Thuc and a large team tune an artificial enzyme by swapping manganese into its crystal. Their study from twenty twenty-six works on zinc cobalt oxide nanozymes. Nanozymes mimic natural enzymes for sensing and catalysis. Oxygen activation limits how fast this one works.
Manganese substitution reshaped the crystal's electronic structure. More mixed-valence states appeared at the particle surface. Oxygen activation and electron transfer both sped up. Binding strength and top speed improved in kinetic tests. The best version beat the pure oxide clearly. Understanding why guides rational nanozyme design. Catalysis improves by editing single atomic positions.
Catalog record
| CREATOR | Duong Hoang Thuc, Vu Thi Huong Mai, Chu Quynh Mai, Pham-Cong De, Van Tan Tran, Vinh Ya, Quoc Huy Thi, Xuan-Dinh Ngo, Van-Tuan Hoang, Anh-Tuan Le |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 50 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |