Computational Study of the Structural and Electronic Properties of Dopant Ions in Microporous AlPOs. 1. Acid Catalytic Activity of Divalent Metal Ions

2003 ◽  
Vol 107 (13) ◽  
pp. 3003-3011 ◽  
Author(s):  
Iman Saadoune ◽  
Furio Corà ◽  
C. Richard A. Catlow
Keyword(s):  
Catalytic Activity ◽  
Metal Ions ◽  
Electronic Properties ◽  
Computational Study ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Structural And Electronic Properties

Catalytic Activity of Cu Ion-Exchanged Metalloaluminophosphates in NO Decomposition

1998 ◽  
Vol 63 (11) ◽  
pp. 1755-1768 ◽  
Author(s):  
Jiří Dědeček ◽  
Alena Vondrová ◽  
Jiří Čejka
Keyword(s):  
Catalytic Activity ◽  
Metal Ions ◽  
Molecular Sieves ◽  
Molecular Sieve ◽  
Negative Charge ◽  
Divalent Metal ◽  
No Decomposition ◽  
Divalent Metal Ions ◽  
Cu Ions

NO decomposition was investigated over Cu ion-exchanged aluminophosphate molecular sieve catalysts. Cu ions in cationic positions balanced by one framework negative charge in the metalloaluminophosphates of AlPO-5 and AlPO-11 structures exhibited catalytic activity in NO decomposition comparable with that of Cu-ZSM-5. No catalytic activity of the Cu ions incorporated during synthesis of molecular sieves into the framework in tetrahedral positions (CuAlPO-11) was observed. The catalytic activity of Cu-MeAlPO-5 and Cu-MeAlPO-11 was observed with various divalent metal ions of the MeAlPO-5 and MeAlPO-11 frameworks (Me = Zn, Mg, Fe, Co) and also with Cu exchanged SAPO-5 molecular sieves. The Cu-MeAlPO-5 and Cu-MeAlPO-11 catalysts differed only in the temperature of the maximum observed catalytic activity.

Interaction of divalent metal ions with the NADP+-malic enzyme from maize leaves

1991 ◽  
Vol 81 (4) ◽  
pp. 462-466 ◽  
Author(s):  
Maria Fabiana Drincovich ◽  
Alberto A. Iglesias ◽  
Carlos S. Andreo
Keyword(s):  
Metal Ions ◽  
Malic Enzyme ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Maize Leaves

scholarly journals Regulation of divalent metal ions to the aggregation and membrane damage of human islet amyloid polypeptide oligomers

RSC Advances ◽  
2021 ◽  
Vol 11 (21) ◽  
pp. 12815-12825
Author(s):  
Yajie Wang ◽  
Feihong Meng ◽  
Tong Lu ◽  
Chunyun Wang ◽  
Fei Li
Keyword(s):  
Metal Ions ◽  
Metal Binding ◽  
Membrane Damage ◽  
Islet Amyloid Polypeptide ◽  
Divalent Metal ◽  
Human Islet ◽  
Divalent Metal Ions ◽  
Islet Amyloid ◽  
Induced Membrane ◽  
Human Islet Amyloid Polypeptide

Their is a counteraction between a decrease in the disruptive ability of metal-associated oligomer species and an increase in the quantity of oligomers promoted by the metal binding in the activity of hIAPP induced membrane damage.

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