Some cellular enzymatic pathways are located within a single organelle, while most others involve enzymes that are located within multiple compartmentalized cellular organelles to realize the efficient multi‐step enzymatic process. Herein, bioinspired by enzyme‐mediated biosynthesis and biochemical defense, a compartmented nanoreactor (Burr‐NCs@GlSOD) was constructed through a self‐confined catalysis strategy with burr defect‐engineered molybdenum disulfide/Prussian blue analogues (MoS2/PBA) and an interfacial diffusion‐controlled hydrogel network. The specific catalytic mechanism of the laccase‐like superactivity induced hydrogelation and cascade enzyme catalytic therapy were explored. The confined hydrogelation strategy introduces a versatile means for nanointerface functionalization and provides insight into biological construction of simulated enzymes with comparable activity and also the specificity to natural enzymes.

Developing cost-effective, active, and robust oxygen evolution reaction (OER) electrocatalysts in alkaline electrolytes is a critical problem in the efficient conversion of renewable energy resources. Here, 3D bicontinuous Mo-doped nanoporous NiFe oxide nanowires (Ni1.4Fe1.7Mo0.05O4) fabricated by eutectic solidification and two-step dealloying exhibit an efficient electrocatalytic OER performance. The resultant nanoporous catalyst can achieve an exceptional activity with a low overpotential (205 mV at 10 mA cm–2) and a small Tafel slope (51.3 mV dec–1), outperforming most of the NiFe-based benchmarks. X-ray absorption spectroscopy combined with density functional theory calculations reveals that strong coupling between the Mo–Fe(Ni)–O sites and its remarkable lattice contraction facilitate the electron transfer on the tiny ligament surface, where the high-valent Mo sites can absorb H2O molecules and lower the energy barrier of OOH* for adsorption and activation of H2O. Meanwhile, 1-D nanowire and 3-D bicontinuous nanoporous structures together with the optimized atom ratio of Fe and Ni can accelerate electron/ion transport in the OER process, thus further enhancing the OER performance.

Some cellular enzymatic pathways are located within a single organelle, while most others involve enzymes that are located within multiple compartmentalized cellular organelles to realize the efficient multi‐step enzymatic process. Herein, bioinspired by enzyme‐mediated biosynthesis and biochemical defense, a compartmented nanoreactor (Burr‐NCs@GlSOD) was constructed through a self‐confined catalysis strategy with burr defect‐engineered molybdenum disulfide/Prussian blue analogues (MoS2/PBA) and an interfacial diffusion‐controlled hydrogel network. The specific catalytic mechanism of the laccase‐like superactivity induced hydrogelation and cascade enzyme catalytic therapy were explored. The confined hydrogelation strategy introduces a versatile means for nanointerface functionalization and provides insight into biological construction of simulated enzymes with comparable activity and also the specificity to natural enzymes.