Catalytic Mechanism for the Ruthenium-Complex-Catalyzed Synthesis of Amides from Alcohols and Amines: A DFT Study

2013 ◽  
Vol 32 (16) ◽  
pp. 4571-4576 ◽  
Author(s):  
Daeheum Cho ◽  
Kyoung Chul Ko ◽  
Jin Yong Lee
Keyword(s):  
Catalytic Mechanism ◽  
Ruthenium Complex ◽  
Dft Study

DFT Study of Hydride Exchange in a Binuclear Ruthenium Complex

2007 ◽  
Vol 26 (1) ◽  
pp. 56-64 ◽  
Author(s):  
Samat Tussupbayev ◽  
Sergei F. Vyboishchikov
Keyword(s):  
Ruthenium Complex ◽  
Dft Study

Catalytic mechanism and pathways of 1, 2-dichloropropane oxidation over LaMnO3 perovskite: An experimental and DFT study

2021 ◽  
Vol 402 ◽  
pp. 123473 ◽  
Author(s):  
Chuanhui Zhang ◽  
Haijie Cao ◽  
Chao Wang ◽  
Maoxia He ◽  
Wangcheng Zhan ◽  
...  
Keyword(s):  
Catalytic Mechanism ◽  
Dft Study

Density functional investigations on the catalytic cycle of the hydrogenation of aldehydes catalyzed by an enhanced ruthenium complex: an alcohol-bridged autocatalytic process

RSC Advances ◽  
2015 ◽  
Vol 5 (4) ◽  
pp. 2827-2836 ◽  
Author(s):  
Xi Lu ◽  
Qian Liu ◽  
Xiaoyin Wang ◽  
Runjiao Cheng ◽  
Mingtao Zhang ◽  
...  
Keyword(s):  
Density Functional ◽  
Ruthenium Complex ◽  
Catalytic Cycle ◽  
Dft Study ◽  
Ru Complex ◽  
Autocatalytic Process

A DFT study of the catalytic cycle of PhCHO hydrogenation catalyzed by Casey’s Ru-complex.

On the Catalytic Mechanism of (S)-2-Hydroxypropylphosphonic Acid Epoxidase (HppE): A Hybrid DFT Study

2012 ◽  
Vol 19 (2) ◽  
pp. 771-781 ◽  
Author(s):  
Anna Miłaczewska ◽  
Ewa Broclawik ◽  
Tomasz Borowski
Keyword(s):  
Catalytic Mechanism ◽  
Dft Study

Influence of chlorine coordination number on the catalytic mechanism of ruthenium chloride catalysts in the acetylene hydrochlorination reaction: a DFT study

2015 ◽  
Vol 17 (12) ◽  
pp. 7720-7730 ◽  
Author(s):  
You Han ◽  
Mengxia Sun ◽  
Wei Li ◽  
Jinli Zhang
Keyword(s):  
Coordination Number ◽  
Catalytic Mechanism ◽  
Dft Study ◽  
Acetylene Hydrochlorination ◽  
Ruthenium Chloride

Among Ru3Cl9, Ru3Cl7, Ru5Cl7, Ru3Cl3 and Ru3 catalytic models, Ru5Cl7 performs best. In Ru5Cl7, the low chloride-coordinated Ru is responsible for activating reactants and adding H to C2H2, while the high coordinated is responsible for providing Cl to C2H3˙.

DFT study on the iridium-catalyzed multi-alkylation of alcohol with ammonia

RSC Advances ◽  
2016 ◽  
Vol 6 (90) ◽  
pp. 87362-87372 ◽  
Author(s):  
Dan-Dan Zhang ◽  
Xian-Kai Chen ◽  
Hui-Ling Liu ◽  
Xu-Ri Huang
Keyword(s):  
Density Functional Theory ◽  
Density Functional ◽  
Catalytic Mechanism ◽  
Water Soluble ◽  
Dft Study ◽  
Functional Theory ◽  
Benzyl Alcohols

The catalytic mechanism for the multi-alkylation of benzyl alcohols with ammonia catalyzed by the water-soluble catalyst, [Cp*IrIII(NH3)3][I]2, is computationally investigated by density functional theory (DFT).

Structures of c-di-GMP/cGAMP degrading phosphodiesterase VcEAL: identification of a novel conformational switch and its implication

2019 ◽  
Vol 476 (21) ◽  
pp. 3333-3353 ◽  
Author(s):  
Malti Yadav ◽  
Kamalendu Pal ◽  
Udayaditya Sen
Keyword(s):  
Active Site ◽  
Metal Binding ◽  
Metal Ion ◽  
Triosephosphate Isomerase ◽  
Catalytic Mechanism ◽  
Degradation Mechanism ◽  
Structural Basis ◽  
Conserved Residues ◽  
Phosphodiester Bond ◽  
Cyclic Dinucleotides

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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