Dual- vs single-active site mechanism in the catalytic decomposition of hydrogen peroxide

1978 ◽  
Vol 40 (6) ◽  
pp. 1277-1278 ◽  
Author(s):  
Mario Barteri ◽  
Marcello Farinella ◽  
Basilio Pispisa
Keyword(s):  
Hydrogen Peroxide ◽  
Active Site ◽  
Catalytic Decomposition

scholarly journals Iron-Imprinted Single-Atomic Site Catalyst-Based Nanoprobe for Detection of Hydrogen Peroxide in Living Cells

2021 ◽  
Vol 13 (1) ◽  
Author(s):  
Zhaoyuan Lyu ◽  
Shichao Ding ◽  
Maoyu Wang ◽  
Xiaoqing Pan ◽  
Zhenxing Feng ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Active Site ◽  
Single Atom ◽  
Site Structure ◽  
Atomic Site ◽  
Ion Imprinting ◽  
Active Site Structure ◽  
In Situ Detection ◽  
Colorimetric Biosensing

AbstractFe-based single-atomic site catalysts (SASCs), with the natural metalloproteases-like active site structure, have attracted widespread attention in biocatalysis and biosensing. Precisely, controlling the isolated single-atom Fe-N-C active site structure is crucial to improve the SASCs’ performance. In this work, we use a facile ion-imprinting method (IIM) to synthesize isolated Fe-N-C single-atomic site catalysts (IIM-Fe-SASC). With this method, the ion-imprinting process can precisely control ion at the atomic level and form numerous well-defined single-atomic Fe-N-C sites. The IIM-Fe-SASC shows better peroxidase-like activities than that of non-imprinted references. Due to its excellent properties, IIM-Fe-SASC is an ideal nanoprobe used in the colorimetric biosensing of hydrogen peroxide (H2O2). Using IIM-Fe-SASC as the nanoprobe, in situ detection of H2O2 generated from MDA-MB-231 cells has been successfully demonstrated with satisfactory sensitivity and specificity. This work opens a novel and easy route in designing advanced SASC and provides a sensitive tool for intracellular H2O2 detection.

Characterisation of a haem active-site mutant of horseradish peroxidase, Phe41 Val, with altered reactivity towards hydrogen peroxide and reducing substrates

1992 ◽  
Vol 207 (2) ◽  
pp. 507-519 ◽  
Author(s):  
Andrew T. SMITH ◽  
Stephen A. SANDERS ◽  
Roger N. F. THORNELEY ◽  
Julian F. BURKE ◽  
Robert R. C. BRAY
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Active Site

Identifying the active site of ultrathin NiCo LDH as an efficient peroxidase mimic with superior substrate affinity for sensitive detection of hydrogen peroxide

2019 ◽  
Vol 7 (40) ◽  
pp. 6232-6237 ◽  
Author(s):  
Yue Sun ◽  
Hai Xu ◽  
Xi Zhao ◽  
Zengyu Hui ◽  
Chenyang Yu ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Active Site ◽  
Colorimetric Detection ◽  
Sensitive Detection ◽  
Substrate Affinity ◽  
Peroxidase Mimic

Ultra-thin NiCo LDH was synthesized as a nanozyme for sensitive colorimetric detection of H2O2 and its active site was identified.

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