Alkali-driven active site shift of fast SCR with NH3 on V2O5–WO3/TiO2 catalyst via a novel Eley–Rideal mechanism

2019 ◽  
Vol 9 (21) ◽  
pp. 6085-6091 ◽  
Author(s):  
Jinyao Xiang ◽  
Xuesen Du ◽  
Yuyi Wan ◽  
Yanrong Chen ◽  
Jingyu Ran ◽  
...  

The heterogeneous SCR reaction obeys the well-known Eley–Rideal mechanism or Langmuir–Hinshelwood mechanism, while fast SCR over alkali-doping catalysts follows the another “E–R” mechanism with adsorbed NO2.

Catalysts ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 618
Author(s):  
Huan Du ◽  
Zhitao Han ◽  
Xitian Wu ◽  
Chenglong Li ◽  
Yu Gao ◽  
...  

Er-modified FeMn/TiO2 catalysts were prepared through the wet impregnation method, and their NH3-SCR activities were tested. The results showed that Er modification could obviously promote SO2 resistance of FeMn/TiO2 catalysts at a low temperature. The promoting effect and mechanism were explored in detail using various techniques, such as BET, XRD, H2-TPR, XPS, TG, and in-situ DRIFTS. The characterization results indicated that Er modification on FeMn/TiO2 catalysts could increase the Mn4+ concentration and surface chemisorbed labile oxygen ratio, which was favorable for NO oxidation to NO2, further accelerating low-temperature SCR activity through the “fast SCR” reaction. As fast SCR reaction could accelerate the consumption of adsorbed NH3 species, it would benefit to restrain the competitive adsorption of SO2 and limit the reaction between adsorbed SO2 and NH3 species. XPS results indicated that ammonium sulfates and Mn sulfates formed were found on Er-modified FeMn/TiO2 catalyst surface seemed much less than those on FeMn/TiO2 catalyst surface, suggested that Er modification was helpful for reducing the generation or deposition of sulfate salts on the catalyst surface. According to in-situ DRIFTS the results of, the presence of SO2 in feeding gas imposed a stronger impact on the NO adsorption than NH3 adsorption on Lewis acid sites of Er-modified FeMn/TiO2 catalysts, gradually making NH3-SCR reaction to proceed in E–R mechanism rather than L–H mechanism. DRIFTS.


2018 ◽  
Vol 557 ◽  
pp. 46-54 ◽  
Author(s):  
Li Cao ◽  
Lei Chen ◽  
Xiaodong Wu ◽  
Rui Ran ◽  
Tengfei Xu ◽  
...  

2018 ◽  
Vol 42 (24) ◽  
pp. 20190-20196 ◽  
Author(s):  
Bo Zhao ◽  
Jun Han ◽  
Linbo Qin ◽  
Wangsheng Chen ◽  
Zijian Zhou ◽  
...  

Mercury oxidation by HCl over V2O5–MoO3/TiO2 followed the Langmuir–Hinshelwood mechanism and showed resistance to SO2.


Author(s):  
Kathleen B. Reuter

The reaction rate and efficiency of piperazine to 1,4-diazabicyclo-octane (DABCO) depends on the Si/Al ratio of the MFI topology catalysts. The Al was shown to be the active site, however, in the Si/Al range of 30-200 the reaction rate increases as the Si/Al ratio increases. The objective of this work was to determine the location and concentration of Al to explain this inverse relationship of Al content with reaction rate.Two silicalite catalysts in the form of 1/16 inch SiO2/Al2O3 bonded extrudates were examined: catalyst A with a Si/Al of 83; and catalyst B, the acid/phosphate Al extracted form of catalyst A, with a Si/Al of 175. Five extrudates from each catalyst were fractured in the transverse direction and particles were obtained from the fracture surfaces near the center of the extrudate diameter. Particles were also obtained from the outside surfaces of five extrudates.


2019 ◽  
Vol 476 (21) ◽  
pp. 3333-3353 ◽  
Author(s):  
Malti Yadav ◽  
Kamalendu Pal ◽  
Udayaditya Sen

Cyclic dinucleotides (CDNs) have emerged as the central molecules that aid bacteria to adapt and thrive in changing environmental conditions. Therefore, tight regulation of intracellular CDN concentration by counteracting the action of dinucleotide cyclases and phosphodiesterases (PDEs) is critical. Here, we demonstrate that a putative stand-alone EAL domain PDE from Vibrio cholerae (VcEAL) is capable to degrade both the second messenger c-di-GMP and hybrid 3′3′-cyclic GMP–AMP (cGAMP). To unveil their degradation mechanism, we have determined high-resolution crystal structures of VcEAL with Ca2+, c-di-GMP-Ca2+, 5′-pGpG-Ca2+ and cGAMP-Ca2+, the latter provides the first structural basis of cGAMP hydrolysis. Structural studies reveal a typical triosephosphate isomerase barrel-fold with substrate c-di-GMP/cGAMP bound in an extended conformation. Highly conserved residues specifically bind the guanine base of c-di-GMP/cGAMP in the G2 site while the semi-conserved nature of residues at the G1 site could act as a specificity determinant. Two metal ions, co-ordinated with six stubbornly conserved residues and two non-bridging scissile phosphate oxygens of c-di-GMP/cGAMP, activate a water molecule for an in-line attack on the phosphodiester bond, supporting two-metal ion-based catalytic mechanism. PDE activity and biofilm assays of several prudently designed mutants collectively demonstrate that VcEAL active site is charge and size optimized. Intriguingly, in VcEAL-5′-pGpG-Ca2+ structure, β5–α5 loop adopts a novel conformation that along with conserved E131 creates a new metal-binding site. This novel conformation along with several subtle changes in the active site designate VcEAL-5′-pGpG-Ca2+ structure quite different from other 5′-pGpG bound structures reported earlier.


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