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Updated: Aug 5, 2026

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
Published on: October 3, 2018
Axial directional orbital buffering of intermediate-induced electronic perturbations enables catalase-coupled oxygen
Jiachen Zhang1,2, Xuezhi Chen3, Yimin Mou1
1State Key Laboratory of Microbial Technology, Jiangsu Key Laboratory of Long-Duration Energy Storage Technology, Jiangsu Collaborative Innovation Centre of Biomedical Functional Materials, School of Chemistry and Materials Science, Nanjing Normal University Nanjing 210023 P.R. China hanjun.sun@njnu.edu.cn.
Abstract:
Metalloenzymes, particularly heme-based enzymes, achieve multifunctional intermediate regulation by leveraging axial ligation, a capability that remains difficult in synthetic single-atom catalysts (SACs) typically optimized for single function. Inspired by natural heme, we propose a directional orbital buffering strategy to couple catalase (CAT)-like reactivity with electrocatalytic oxygen reduction reaction (ORR). Among the examined iron-nitrogen-carbon (Fe-N-C) catalysts, axially coordinated FeN5-C exhibits the highest H2O2 decomposition efficiency (K cat/K m = 0.41 mM-1 s-1), converting H2O2 to O2. Mechanistic analyses reveal that FeN5-C enables directional orbital buffering and balanced oxygen-intermediate turnover, allowing ORR-generated H2O2 to enter the CAT-like pathway and regenerate O2 for in situ ORR at the same active site. Consequently, FeN5-C achieves an ultralow H2O2 yield of 0.41% and enhanced ORR activity in neutral media. As a membrane-free glucose/O2 biofuel-cell cathode, FeN5-C delivers exceptional H2O2 resistance and a record power density.
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