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Heme Cofactor‐Resembling Fe–N Single Site Embedded Graphene as Nanozymes to Selectively Detect H 2 O 2 with High Sensitivity
Author(s) -
Kim Min Su,
Lee Junsang,
Kim Hye Su,
Cho Ara,
Shim Kyu Hwan,
Le Thao Nguyen,
An Seong Soo A.,
Han Jeong Woo,
Kim Moon Il,
Lee Jinwoo
Publication year - 2020
Publication title -
advanced functional materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.069
H-Index - 322
eISSN - 1616-3028
pISSN - 1616-301X
DOI - 10.1002/adfm.201905410
Subject(s) - catalysis , selectivity , graphene , cofactor , oxidizing agent , active site , horseradish peroxidase , heme , peroxidase , rational design , combinatorial chemistry , materials science , chemistry , transition metal , nanotechnology , enzyme , organic chemistry
Over the past decade, the catalytic activity of nanozymes has been greatly enhanced, but their selectivity is still low and considered a critical issue to overcome. Herein, Fe–N 4 single site embedded graphene (Fe–N‐rGO), which resembles the heme cofactor present in natural horseradish peroxidase, shows a marked enhancement in peroxidase‐like catalytic efficiency of up to ≈700‐fold higher than that of undoped rGO as well as excellent selectivity toward target H 2 O 2 without any oxidizing activity. Importantly, when Fe or N is doped alone or when Fe is replaced with another transition metal in the Fe–N 4 site, the activity is negligibly enhanced, showing that mimicking the essential cofactor structure of natural enzyme might be essential to design the catalytic features of nanozymes. Density functional theory results for the change in Gibbs free energy during the peroxide decomposition reaction explain the high catalytic activity of Fe–N‐rGO. Based on the high and selective peroxidase‐like activity of Fe–N‐rGO, trace amounts of H 2 O 2 produced from the enzymatic reactions from acetylcholine and cancerous cells are successfully quantified with high sensitivity and selectivity. This work is expected to encourage studies on the rational design of nanozymes pursuing the active site structure of natural enzymes.