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Herein, ammonium (NH4+)-intercalated \u03b4-MnO2 nanozymes (N-MnO2) were constructed through the acid\u2013base neutralization strategy. Due to interlayer van der Waals interactions, the NH4+ is stabilized in a nonbonded configuration. Significantly, nonbonding NH4+ exhibits unique electron-manipulating capabilities, enabling precise regulation of Mn 3d spin electrons from a high-spin state (t2g3eg1) to low-spin (t2g4eg0) configurations. The controlled spin-state redistribution prevents electron occupation in the eg antibonding orbitals (\u03c3*), thereby significantly enhancing the stability of the Mn\u2013O \u03c3-bond and suppressing Jahn\u2013Teller (J-T) distortions in the [MnO6] octahedra of layered MnO2. This dual nonbonding stabilization mechanism effectively resists structural disruption by endogenous glutathione (GSH, a scavenger of superoxide radicals), which can enhance the enzyme-mimetic activity. Furthermore, the nonbonding NH4+ in N-MnO2 maintains a dynamic Mn3+\/Mn4+ equilibrium, endowing the nanozyme with dual catalase-like and oxidase-like activities. This can catalyze cascade enzymatic reactions (H2O2 \u2192 O2 \u2192 O2\u2022\u2013) to sufficiently enrich O2\u2022\u2013. Consequently, it is demonstrated that N-MnO2 possesses enhanced cascade catalytic performance within the complex TME for tumor-specific therapy.<\/jats:p>","DOI":"10.1021\/jacs.6c02992","type":"journal-article","created":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T08:03:48Z","timestamp":1778745828000},"page":"23865-23878","source":"Crossref","is-referenced-by-count":3,"title":["Nonbonding Ammonium\nStabilizing Manganese\u2013Oxygen\n\u03c3-Bond by Manipulating Spin Electrons to Regulate Enzymatic\nActivities"],"prefix":"10.1021","volume":"148","author":[{"given":"Qi","family":"Zhao","sequence":"first","affiliation":[{"name":"Beijing Normal University , , ,","place":["Beijing, China, 100875"]},{"name":"Jilin University , , ,","place":["Changchun, P. R. 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