School of Mechanical and Materials Engineering, Washington State University, Pullman, WA, 99164, USA.
Department of Chemistry and Biochemistry, Northern Illinois University, DeKalb, IL, 60115, USA.
Small. 2021 Jun;17(25):e2100664. doi: 10.1002/smll.202100664. Epub 2021 May 24.
Heme enzymes, with the pentacoordinate heme iron active sites, possess high catalytic activity and selectivity in biosensing applications. However, they are still subject to limited catalytic stability in the complex environment and high cost for broad applications in electrochemical sensing. It is meaningful to develop a novel substitute that has a similar structure to some heme enzymes and mimics their enzyme activities. One emerging strategy is to design the Fe-N-C based single-atomic site catalysts (SASCs). The obtained atomically dispersed Fe-N active sites can mimic the active sites of heme enzymes effectively. In this work, a SASC (Fe-SASC/NW) is synthesized by doping single iron atoms in polypyrrole (PPy) derived carbon nanowire via a zinc-atom-assisted method. The proposed Fe-SASC/NW shows high heme enzyme-like catalytic performance for hydrogen peroxide (H O ) with a specific activity of 42.8 U mg . An electrochemical sensor based on Fe-SASC/NW is developed for the detection of H O . This sensor exhibits a wide detection concentration range from 5.0 × 10 m to 0.5 m and an excellent limit of detection (LOD) of 46.35 × 10 m. Such excellent catalytic activity and electrochemical sensing sensitivity are attributed to the isolated Fe-N active sites and their structural similarity with natural metalloproteases.
血红素酶具有五配位的血红素铁活性中心,在生物传感应用中具有高催化活性和选择性。然而,它们在复杂环境中的催化稳定性仍然有限,并且电化学传感的广泛应用成本高昂。因此,开发一种具有类似结构且模拟其酶活性的新型替代物具有重要意义。一种新兴的策略是设计基于 Fe-N-C 的单原子位点催化剂 (SASCs)。所获得的原子分散的 Fe-N 活性位点可以有效地模拟血红素酶的活性位点。在这项工作中,通过锌原子辅助的方法,在聚吡咯(PPy)衍生的碳纳米线中掺杂单个铁原子,合成了一种 SASC(Fe-SASC/NW)。所提出的 Fe-SASC/NW 对过氧化氢(H 2 O 2 )表现出高血红素酶样催化性能,比活性为 42.8 U mg -1 。基于 Fe-SASC/NW 开发了用于检测 H 2 O 2 的电化学传感器。该传感器具有从 5.0 × 10 -6 到 0.5 m 的宽检测浓度范围和优异的检测限(LOD)为 46.35 × 10 -6 m。这种优异的催化活性和电化学传感灵敏度归因于孤立的 Fe-N 活性位点及其与天然金属蛋白酶的结构相似性。