A theoretic insight into the catalytic activity promotion of CeO2 surfaces by Mn doping

2012 ◽  
Vol 14 (16) ◽  
pp. 5769 ◽  
Author(s):  
Wanglai Cen ◽  
Yue Liu ◽  
Zhongbiao Wu ◽  
Haiqiang Wang ◽  
Xiaole Weng
Chem ◽  
2018 ◽  
Vol 4 (3) ◽  
pp. 613-625 ◽  
Author(s):  
Yuhan Peng ◽  
Liangbing Wang ◽  
Qiquan Luo ◽  
Yun Cao ◽  
Yizhou Dai ◽  
...  

ACS Nano ◽  
2018 ◽  
Vol 12 (12) ◽  
pp. 12169-12180 ◽  
Author(s):  
Weitao Yang ◽  
Xiudong Shi ◽  
Yuxin Shi ◽  
Defan Yao ◽  
Shizhen Chen ◽  
...  

Author(s):  
Maria Laura Soriano

A new tendency toward the design of artificial enzymes based on nanostructures (nanodots, nanofibers, mesoporous materials) has emerged. On one hand, nanotechnology bestows self-catalytic nanoparticles with a specific activity to achieve efficient reactions with low number of by-products. On other hand, the nanoparticles may behave as nanometric scaffolds for hosting enzymes, promoting their catalytic activity and stability. In this case, enzyme immobilization requires the preservation of the catalytic activity by preventing enzyme unfolding and avoiding its aggregation. These approaches render many other advantages like hosting/storing enzymes in nanotechnological solid, liquid, and gel-like media. This chapter focuses on the most up-to-date approaches to manipulate or mimic enzyme activity based on nanotechnology, and offers examples of their applications in the most promising fields. It also gives new insight into the creation of reusable nanotechnological tools for enzyme storage.


2015 ◽  
Vol 492 ◽  
pp. 1-9 ◽  
Author(s):  
Huawen Hu ◽  
John H. Xin ◽  
Hong Hu ◽  
Xiaowen Wang ◽  
Yeeyee Kong

2018 ◽  
Vol 6 (20) ◽  
pp. 9467-9472 ◽  
Author(s):  
Jianwen Huang ◽  
Ying Su ◽  
Yadong Zhang ◽  
Wenqi Wu ◽  
Chunyang Wu ◽  
...  

The introduction of the FeOx/FeP interface effect not only facilitates the water adsorption and dissociation in neutral HER, but also modifies the ΔG(H*) of FeP, exhibiting remarkable catalytic activity with a Tafel slope as low as 47 mV dec−1.


2020 ◽  
Vol 13 (1) ◽  
Author(s):  
Yiqi Yang ◽  
Gang Li

Abstract Polycomb repressive complex 2 (PRC2) is a chromatin-modifying enzyme that catalyses the methylation of histone H3 at lysine 27 (H3K27me1/2/3). This complex maintains gene transcriptional repression and plays an essential role in the maintenance of cellular identity as well as normal organismal development. The activity of PRC2, including its genomic targeting and catalytic activity, is controlled by various signals. Recent studies have revealed that these signals involve cis chromatin features, PRC2 facultative subunits and post-translational modifications (PTMs) of PRC2 subunits. Overall, these findings have provided insight into the biochemical signals directing PRC2 function, although many mysteries remain.


2020 ◽  
Vol 4 (6) ◽  
pp. 2741-2751
Author(s):  
Fei Jiang ◽  
Ke Qu ◽  
Mingshan Wang ◽  
Junchen Chen ◽  
Yang Liu ◽  
...  

Mn doping could form a stable LiMnxFe1−xPO4 protective shell on the surface to suppress LiFePO4 degradation during electrochemical cycling.


2020 ◽  
Vol 10 (1) ◽  
pp. 169-179 ◽  
Author(s):  
Li Zhou ◽  
Datai Liu ◽  
Haiyi Lan ◽  
Xiujian Wang ◽  
Cunyuan Zhao ◽  
...  

The origin of different catalytic activity between two structurally similar Lewis basic bifunctional catalysts.


2017 ◽  
Vol 19 (26) ◽  
pp. 17449-17460 ◽  
Author(s):  
Guixia Li ◽  
Lianming Zhao ◽  
Houyu Zhu ◽  
Xiuping Liu ◽  
Huifang Ma ◽  
...  

Surface S shows a promotion effect on the HDS catalytic activity of MoP(010) by lowering the C–S bond scission energy barrier.


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