Reversible CO2 Activation by a N-Phosphinoamidinato Digermyne

2022 ◽  
Author(s):  
Cheuk-Wai So ◽  
Jun Fan ◽  
Shina Quek ◽  
Ming-Chung Yang ◽  
Zheng-Feng Zhang ◽  
...  
Keyword(s):  
Co2 Activation

The N-phosphinoamidinato digermynes [LË–ËL] (E = Ge, L = tBu2PNC(Ph)NAr, 4: Ar = 2,6-iPr2C6H3, 5: Ar = Ph) underwent reversible CO2 activation to form [LËOC(O)ËL] (6: Ar = 2,6-iPr2C6H3, 7:...

Efficient photocatalytic CO2 reformation of methane on Ru/La‐g‐C3N4 by promoting charge transfer and CO2 activation

ChemPhotoChem ◽  
2021 ◽  
Author(s):  
Naixu Li ◽  
Xianhe Li ◽  
Rui Pan ◽  
Miao Cheng ◽  
Jie Guan ◽  
...  
Keyword(s):  
Charge Transfer ◽  
Co2 Activation

scholarly journals Theoretical Study on the Degree of CO2 Activation in CO2-Coordinated Ni(0) Complexes

ACS Omega ◽  
2021 ◽  
Author(s):  
Joonho Park ◽  
Moses Cho ◽  
Young Min Rhee ◽  
Yousung Jung
Keyword(s):  
Theoretical Study ◽  
Co2 Activation

Engineering the Active Sites of Graphene Catalyst: From CO2 Activation to Activate Li-CO2 Batteries

ACS Nano ◽  
2021 ◽  
Author(s):  
Biao Chen ◽  
Dashuai Wang ◽  
Biao Zhang ◽  
Xiongwei Zhong ◽  
Yingqi Liu ◽  
...  
Keyword(s):  
Active Sites ◽  
Co2 Activation

scholarly journals From CO2 activation to catalytic reduction: a metal-free approach

2020 ◽  
Vol 11 (39) ◽  
pp. 10571-10593 ◽  
Author(s):  
Sreejyothi P. ◽  
Swadhin K. Mandal
Keyword(s):  
Catalytic Reduction ◽  
Review Article ◽  
Co2 Activation ◽  
Metal Free

This review article documents the key developments in the metal-free catalytic reduction of CO2 into various energy intensive chemicals and fuels, and reductive functionalization of CO2 for the formation of new C–N bonds.

scholarly journals CO2 Activation and Hydrogenation by PtH n − Cluster Anions

2016 ◽  
Vol 128 (33) ◽  
pp. 9796-9799 ◽  
Author(s):  
Xinxing Zhang ◽  
Gaoxiang Liu ◽  
Karl-Heinz Meiwes-Broer ◽  
Gerd Ganteför ◽  
Kit Bowen
Keyword(s):  
Co2 Activation ◽  
Cluster Anions

scholarly journals CO2 activation through silylimido and silylamido zirconium hydrides supported on N-donor chelating SBA15 surface ligands

2016 ◽  
Vol 52 (12) ◽  
pp. 2577-2580 ◽  
Author(s):  
Farhan Ahmad Pasha ◽  
Anissa Bendjeriou-Sedjerari ◽  
Edy Abou-Hamad ◽  
Kuo-Wei Huang ◽  
Jean-Marie Basset
Keyword(s):  
Density Functional Theory ◽  
Solid State ◽  
Solid State Nmr ◽  
Density Functional ◽  
Density Functional Theory Calculations ◽  
Co2 Activation ◽  
Functional Theory ◽  
Surface Ligands ◽  
Different Types ◽  
Zirconium Hydrides

Density functional theory calculations and 2D 1H–13C HETCOR solid state NMR spectroscopy prove that CO2 can be used to probe, by its own reactivity, different types of N-donor surface ligands on SBA15-supported ZrIV hydrides: [(Si–O–)(Si–N)[Zr]H] and [(Si–NH–)(Si–X–)[Zr]H2] (XO or NH).

Ab Initio Study of CO2 Activation on Pristine and Fe-Decorated WS2 Nanoflakes

2021 ◽  
Author(s):  
Henrique A. B. Fonseca ◽  
Lucas G. Verga ◽  
Juarez L. F. Da Silva
Keyword(s):  
Ab Initio ◽  
Co2 Activation ◽  
Ab Initio Study

scholarly journals Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase)

1989 ◽  
Vol 261 (1) ◽  
pp. 289-291 ◽  
Author(s):  
P A Deddish ◽  
R A Skidgel ◽  
E G Erdös
Keyword(s):  
Plasma Membrane ◽  
Low Ph ◽  
Co2 Activation ◽  
Inhibitor Binding ◽  
Carboxypeptidase B ◽  
Acid Ph ◽  
Carboxypeptidase H ◽  
Membrane Bound ◽  
Carboxypeptidase N ◽  
Carboxypeptidase M

Carboxypeptidases H and M differ in their distribution and other properties, but both are activated by Co2+ and inhibited by guanidinoethylmercaptosuccinic acid. The higher degree of activation or inhibition of carboxypeptidase H by these agents at acid pH has been employed to identify this enzyme in tissues. We found that the activation or inhibition of both purified and plasma-membrane-bound human carboxy-peptidase M depends on the pH of the medium. CoCl2 activated over 6-fold at pH 5.5, but less than 2-fold at pH 7.5. Guanidinoethylmercaptosuccinic acid inhibited the membrane-bound carboxypeptidase M more effectively than the purified enzyme, and the IC50 was about 25-30 times lower at pH 5.5. As purified human plasma carboxypeptidase N and pancreatic carboxypeptidase B were also activated more at pH 5.5, we conclude that the increased activation by CoCl2 is due to the enhanced dissociation of Zn2+ below the pKa of the ligands that co-ordinate the cofactor in the protein. Thus increased activation or inhibition at acid pH would not differentiate basic carboxypeptidases.

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