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0D-1D hybrid nanoarchitectonics: tailored design of FeCo@N-C yolk-shell nanoreactors with dual sites for excellent Fenton-like catalysis.


ABSTRACT: Heterogeneous Fenton-like processes are very promising methods of treating organic pollutants through the generation of reactive oxygen containing radicals. Herein, we report novel 0D-1D hybrid nanoarchitectonics (necklace-like structures) consisting of FeCo@N-C yolk-shell nanoreactors as advanced catalysts for Fenton-like reactions. Each FeCo@N-C unit possesses a yolk-shell structure like a nanoreactor, which can accelerate the diffusion of reactive oxygen species and guard the active sites of FeCo. Furthermore, all the nanoreactors are threaded along carbon fibers, providing a highway for electron transport. FeCo@N-C nano-necklaces thereby exhibit excellent performance for pollutant removal via activation of peroxymonosulfate, achieving 100% bisphenol A (k = 0.8308 min-1) degradation in 10 min with good cycling stability. The experiments and density-functional theory calculations reveal that FeCo dual sites are beneficial for activation of O-O, which is crucial for enhancing Fenton-like processes.

SUBMITTER: Wang C 

PROVIDER: S-EPMC8635224 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature

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0D-1D hybrid nanoarchitectonics: tailored design of FeCo@N-C yolk-shell nanoreactors with dual sites for excellent Fenton-like catalysis.

Wang Chaohai C   Wang Hongyu H   Na Jongbeom J   Yao Yiyuan Y   Azhar Alowasheeir A   Yan Xin X   Qi Junwen J   Yamauchi Yusuke Y   Li Jiansheng J  

Chemical science 20211111 46


Heterogeneous Fenton-like processes are very promising methods of treating organic pollutants through the generation of reactive oxygen containing radicals. Herein, we report novel 0D-1D hybrid nanoarchitectonics (necklace-like structures) consisting of FeCo@N-C yolk-shell nanoreactors as advanced catalysts for Fenton-like reactions. Each FeCo@N-C unit possesses a yolk-shell structure like a nanoreactor, which can accelerate the diffusion of reactive oxygen species and guard the active sites of  ...[more]

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