scholarly journals Aryl bis-sulfonamides bind to the active site of a homotrimeric isoprenoid biosynthesis enzyme IspF and extract the essential divalent metal cation cofactor

2018 ◽  
Vol 9 (27) ◽  
pp. 5976-5986 ◽  
Author(s):  
Katharina Root ◽  
Konstantin Barylyuk ◽  
Anatol Schwab ◽  
Jonas Thelemann ◽  
Boris Illarionov ◽  
...  
Keyword(s):  
Protein Binding ◽  
Metal Cation ◽  
Active Site ◽  
Divalent Metal ◽  
Isoprenoid Biosynthesis ◽  
Divalent Metal Cation ◽  
Esi Ms ◽  
Binding Mechanisms ◽  
Insight Into

Native ESI-MS delivers unprecedented insight into unknown homomeric protein binding mechanisms involving complex, multistage binding equilibria with cofactors and ligands.

scholarly journals Role of the divalent metal cation in the pyruvate oxidase reaction.

1982 ◽  
Vol 257 (16) ◽  
pp. 9605-9611
Author(s):  
R Blake ◽  
T A O'Brien ◽  
R B Gennis ◽  
L P Hager
Keyword(s):  
Metal Cation ◽  
Divalent Metal ◽  
Pyruvate Oxidase ◽  
Divalent Metal Cation ◽  
Oxidase Reaction

The induction of the acrosome reaction in guinea-pig sperm by the divalent metal cation ionophore A23187

1978 ◽  
Vol 32 (1) ◽  
pp. 137-151
Author(s):  
D.P. Green
Keyword(s):  
Guinea Pig ◽  
Metal Cation ◽  
Acrosome Reaction ◽  
Divalent Metal ◽  
Secretory Cells ◽  
Free Calcium ◽  
Ionophore A23187 ◽  
Divalent Metal Cation ◽  
Free Calcium Concentration ◽  
External Calcium

The divalent metal cation ionophore A23187 induces an acrosome reaction in guinea-pig sperm which is dependent on external calcium. Examination of this acrosome reaction by electron microscopy shows that it is morphologically normal. The known properties of A23187 and the morphological similarity between the acrosome reaction and the secretory discharges of other secretory cells suggests that the immediate cause of the acrosome reaction is an increase in the cytoplasmic free calcium concentration.

Divalent metal cation requirements of phosphofructokinase-2 from E. coli. Evidence for a high affinity binding site for Mn2+

2011 ◽  
Vol 505 (1) ◽  
pp. 60-66 ◽  
Author(s):  
Jaime Andrés Rivas-Pardo ◽  
Andrés Caniuguir ◽  
Christian A.M. Wilson ◽  
Jorge Babul ◽  
Victoria Guixé
Keyword(s):  
Binding Site ◽  
Metal Cation ◽  
Divalent Metal ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
Divalent Metal Cation ◽  
E Coli ◽  
High Affinity ◽  
High Affinity Binding Site

Silicon nitride nanopore created by dielectric breakdown with a divalent cation: deceleration of translocation speed and identification of single nucleotides

Nanoscale ◽  
2019 ◽  
Vol 11 (30) ◽  
pp. 14426-14433 ◽  
Author(s):  
Yusuke Goto ◽  
Kazuma Matsui ◽  
Itaru Yanagi ◽  
Ken-ichi Takeda
Keyword(s):  
Silicon Nitride ◽  
Divalent Cation ◽  
Metal Cation ◽  
Dielectric Breakdown ◽  
Divalent Metal ◽  
Single Stranded Dna ◽  
Divalent Metal Cation ◽  
Translocation Speed

Controlled dielectric breakdown with a divalent metal cation provides a silicon nitride nanopore with the ability to decelerate single-stranded DNA speed.

scholarly journals The structural variety of DNA-DPPC-divalent metal cation aggregates: SAXD and SANS study

2009 ◽  
Vol 167 (1) ◽  
pp. 191-197 ◽  
Author(s):  
D. Uhríková ◽  
P. Pullmannová ◽  
N. Kučerka ◽  
S. S. Funari ◽  
J. Teixeira ◽  
...  
Keyword(s):  
Metal Cation ◽  
Divalent Metal ◽  
Divalent Metal Cation ◽  
Structural Variety
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