Subunit location of the intrinsic divalent metal ions in RNA polymerase from Escherichia coli

Biochemistry ◽  
1977 ◽  
Vol 16 (25) ◽  
pp. 5449-5454 ◽  
Author(s):  
Cheng-Wen Wu ◽  
Felicia Y. H. Wu ◽  
David C. Speckhard
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Metal Ions ◽  
Divalent Metal ◽  
Divalent Metal Ions

L-Aspartase from Escherichia coli: substrate specificity and role of divalent metal ions

Biochemistry ◽  
1988 ◽  
Vol 27 (26) ◽  
pp. 9089-9093 ◽  
Author(s):  
Christopher J. Falzone ◽  
William E. Karsten ◽  
Judith D. Conley ◽  
Ronald E. Viola
Keyword(s):  
Escherichia Coli ◽  
Substrate Specificity ◽  
Metal Ions ◽  
Divalent Metal ◽  
Divalent Metal Ions

scholarly journals Synthesis, Characterization and Biological Activity of Some Mixed Ligand Complexes of 1, 10-Phenanthronline and [4-(2-hydroxy-1,2-diphenylethylideneamino)-N-pyrimidin-2-yl) benzene sulfonamide] with Divalent Metal Ions

2017 ◽  
Vol 27 (5) ◽  
pp. 55
Author(s):  
Rehab K. Al-Shemary ◽  
Inam H. Ibrahim ◽  
Nibras A. Al-marsomy
Keyword(s):  
Escherichia Coli ◽  
Metal Ions ◽  
Acidic Medium ◽  
Condensation Reaction ◽  
Divalent Metal ◽  
Mixed Ligand ◽  
Mixed Ligand Complexes ◽  
Divalent Metal Ions ◽  
Ft Ir ◽  
And Staphylococcus Aureus

Schiff base ligand [4-(2-hydroxy-1, 2-diphenylethylideneamino)-N-pyrimidin-2-yl)benzene sulfonamide] (L) was prepared through a condensation reaction of  sulfadiazine and benzoin in acidic medium. The prepared ligand has been characterized with different techniques (C.H.N.S, FT-IR, UV-Vis and 1H&13C-N.M.R). Mixed ligand complexes of some divalent metal ions [Co(II), Mn(II), Ni(II),Cu(II) and Hg(II)] were prepared by the  reaction of [4-(2-hydroxy-1,2-diphenylethylidene amino)-N-pyrimidin-2-yl)benzene sulfonamide](L)  and 1,10-Phenanthronline with the metal ions in basic conditions. The prepared complexes were characterized and their astrochemical structures and geometries were suggested depending upon data of (UV-Vis, FT-IR, atomic absorption, micro elemental analysis The following general formula was achieved : [M(PHN)(L)2], where  M represent  (Co(II)- Cu(II)-Mn(II)- Ni(II) and Hg(II)). Electronic spectra supported by magnetic moment's revealed octahedral geometries for all the prepared complexes. The mixed complexes showed resistivity to different bacteria such as(Pseudomonas aeruginosa), (Bacillus subtilis), (Escherichia coli), and (staphylococcus aureus).

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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