Rationally Designed Synthesis of Metal–Organic Framework-Derived Cobalt Oxide with Abundant Surface Active Sites for Efficient Catalytic Oxidation Performance

2020 ◽  
Vol 20 (9) ◽  
pp. 5716-5727
Author(s):  
Weiliang Han ◽  
Zhicheng Tang ◽  
Qi Lin
Author(s):  
Danni Zhou ◽  
Xinyuan Li ◽  
Huishan Shang ◽  
Fengjuan Qin ◽  
Wenxing Chen

Metal-organic framework (MOF) derived single-atom catalysts (SACs), featured unique active sites and adjustable topological structures, exhibit high electrocatalytic performance on carbon dioxide reduction reactions (CO2RR). By modulating elements and atomic...


2019 ◽  
Vol 149 (5) ◽  
pp. 1237-1249 ◽  
Author(s):  
Ahmad Shaabani ◽  
Reza Mohammadian ◽  
Hassan Farhid ◽  
Masoumeh Karimi Alavijeh ◽  
Mostafa M. Amini

2021 ◽  
Author(s):  
Sujing Wang ◽  
Antoine Tissot ◽  
Guillaume Maurin ◽  
Tatjana Parac-Vogt ◽  
Christian Serre ◽  
...  

<div>The discovery of nanozymes for selective cleavage of proteins would boost the emerging areas of modern proteomics, however, the development of efficient and reusable artificial catalysts for peptide bond hydrolysis is challenging. Here we report the detailed catalytic properties of a microporous zirconium carboxylate metal-organic framework, MIP-201, in promoting peptide bond hydrolysis in a simple dipeptide, as well as in horse-heart myoglobin (Mb) protein that consists of 153 amino acids. We demonstrate that MIP-201 features an excellent catalytic activity and selectivity, a good tolerance toward reaction conditions covering a wide range of different pH values, and importantly, an exceptional recycling ability associated with easy regeneration process. Taking into account the excellent catalytic performance of MIP-201 and its other advantages such as 6-connected Zr6 cluster active sites, the green, scalable and cost-effective synthesis, and an outstanding chemical and architectural stability, our finding suggests that MIP-201 may be a promising and practical alternative to the current commercially available catalysts for peptide bond hydrolysis.</div>


2021 ◽  
Author(s):  
Sujing Wang ◽  
Antoine Tissot ◽  
Guillaume Maurin ◽  
Tatjana Parac-Vogt ◽  
Christian Serre ◽  
...  

<div>The discovery of nanozymes for selective cleavage of proteins would boost the emerging areas of modern proteomics, however, the development of efficient and reusable artificial catalysts for peptide bond hydrolysis is challenging. Here we report the detailed catalytic properties of a microporous zirconium carboxylate metal-organic framework, MIP-201, in promoting peptide bond hydrolysis in a simple dipeptide, as well as in horse-heart myoglobin (Mb) protein that consists of 153 amino acids. We demonstrate that MIP-201 features an excellent catalytic activity and selectivity, a good tolerance toward reaction conditions covering a wide range of different pH values, and importantly, an exceptional recycling ability associated with easy regeneration process. Taking into account the excellent catalytic performance of MIP-201 and its other advantages such as 6-connected Zr6 cluster active sites, the green, scalable and cost-effective synthesis, and an outstanding chemical and architectural stability, our finding suggests that MIP-201 may be a promising and practical alternative to the current commercially available catalysts for peptide bond hydrolysis.</div>


2020 ◽  
Vol 496 ◽  
pp. 111196
Author(s):  
Shiye Li ◽  
Lihan Shi ◽  
Li Zhang ◽  
Hongmei Huang ◽  
Yi Xiao ◽  
...  

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