scholarly journals Crystal structure of histidinol phosphate phosphatase: coordination of three metal ions

2004 ◽  
Vol 60 (a1) ◽  
pp. s173-s173
Author(s):  
R. Omi ◽  
M. Goto ◽  
I. Miyahara ◽  
K. Hirotsu
Keyword(s):  
Crystal Structure ◽  
Metal Ions ◽  
Histidinol Phosphate Phosphatase

scholarly journals Nano-Azo Ligand and Its Superhydrophobic Complexes: Synthesis, Characterization, DFT, Contact Angle, Molecular Docking, and Antimicrobial Studies

2020 ◽  
Vol 2020 ◽  
pp. 1-19
Author(s):  
Gehad G. Mohamed ◽  
Walaa H. Mahmoud ◽  
Ahmed M. Refaat
Keyword(s):  
Crystal Structure ◽  
Contact Angle ◽  
Molecular Docking ◽  
Metal Ions ◽  
Metal Complexes ◽  
Biological Activities ◽  
Thermal Studies ◽  
Free Ligand ◽  
Aminobenzoic Acid ◽  
Azo Ligand

Metal complexes of the 2,2'-(1,3-phenylenebis(diazene-2,1-diyl))bis(4-aminobenzoic acid) diazo ligand (H2L) derived from m-phenylenediamine and p-aminobenzoic acid were synthesized and characterized by different spectral, thermal, and analytical tools. The H2L ligand reacted with the metal ions Cr(III), Mn(II), Fe(III), Co(II), Ni(II), Cu(II), Zn(II), and Cd(II) as 1 : 1 stoichiometry. All complexes displayed an octahedral geometry according to the electronic and magnetic moment measurements. The IR spectra revealed the binding of the azo ligand to the metal ions via two azo nitrogen atoms and protonated carboxylate O in a neutral tetradentate manner. Both IR and 1H NMR spectra documented the involvement of the carboxylate group without proton displacement. The thermal studies pointed out that the complexes had higher thermal stability comparable with that of the free ligand. SEM images revealed the presence of the diazo ligand and its Cd(II) complex in a nanostructure form. The contact angle measurements proved that the Cd(II) complex can be considered as a superhydrophobic material. The molecular and electronic structure of H2L and [Cd(H2L)Cl2].H2O were optimized theoretically, and the quantum chemical parameters were calculated. The biological activities of the ligand, as well as its metal complexes, have been tested in vitro against some bacteria and fungi species. The results showed that all the tested compounds have significant biological activities with different sensitivity levels. The binding between H2L and its Cd(II) complex with receptors of the crystal structure of S. aureus (PDB ID: 3Q8U), crystal structure of protein phosphatase (PPZ1) of Candida albicans (PDB ID: 5JPE), receptors of breast cancer mutant oxidoreductase (PDB ID: 3HB5), and crystal structure of Escherichia coli (PDB ID: 3T88) was predicted and given in detail using molecular docking.

Reactions of metal ions with vitamins. IV. The crystal structure of a zinc complex of pyridoxamine (Vitamin B6)

1980 ◽  
Vol 46 ◽  
pp. 199-203 ◽  
Author(s):  
Doris Margaret Thompson ◽  
Walt Balenovich ◽  
Linda H.M. Hornich ◽  
Mary Frances Richardson
Keyword(s):  
Crystal Structure ◽  
Metal Ions ◽  
Vitamin B6 ◽  
Zinc Complex

Complexes of 3d metal ions of the Schiff-base, 4-hydroxy-N′-(4′-octadecyloxybenzylidene)benzohydrazide: Synthesis, spectral studies, crystal structure and magnetic interactions

Polyhedron ◽  
2009 ◽  
Vol 28 (13) ◽  
pp. 2599-2604 ◽  
Author(s):  
Angad Kumar Singh ◽  
Sanyucta Kumari ◽  
K. Ravi Kumar ◽  
B. Sridhar ◽  
Miroslaw Wrzecion ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Schiff Base ◽  
Metal Ions ◽  
Magnetic Interactions ◽  
Spectral Studies

scholarly journals A trapped human PPM1A–phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity

2018 ◽  
Vol 293 (21) ◽  
pp. 7993-8008 ◽  
Author(s):  
Subrata Debnath ◽  
Dalibor Kosek ◽  
Harichandra D. Tagad ◽  
Stewart R. Durell ◽  
Daniel H. Appella ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Metal Ions ◽  
Active Site ◽  
Metal Binding ◽  
Metal Ion ◽  
Catalytic Domain ◽  
Protein Phosphatases ◽  
Random Order ◽  
Structural Features

Metal-dependent protein phosphatases (PPM) are evolutionarily unrelated to other serine/threonine protein phosphatases and are characterized by their requirement for supplementation with millimolar concentrations of Mg2+ or Mn2+ ions for activity in vitro. The crystal structure of human PPM1A (also known as PP2Cα), the first PPM structure determined, displays two tightly bound Mn2+ ions in the active site and a small subdomain, termed the Flap, located adjacent to the active site. Some recent crystal structures of bacterial or plant PPM phosphatases have disclosed two tightly bound metal ions and an additional third metal ion in the active site. Here, the crystal structure of the catalytic domain of human PPM1A, PPM1Acat, complexed with a cyclic phosphopeptide, c(MpSIpYVA), a cyclized variant of the activation loop of p38 MAPK (a physiological substrate of PPM1A), revealed three metal ions in the active site. The PPM1Acat D146E–c(MpSIpYVA) complex confirmed the presence of the anticipated third metal ion in the active site of metazoan PPM phosphatases. Biophysical and computational methods suggested that complex formation results in a slightly more compact solution conformation through reduced conformational flexibility of the Flap subdomain. We also observed that the position of the substrate in the active site allows solvent access to the labile third metal-binding site. Enzyme kinetics of PPM1Acat toward a phosphopeptide substrate supported a random-order, bi-substrate mechanism, with substantial interaction between the bound substrate and the labile metal ion. This work illuminates the structural and thermodynamic basis of an innate mechanism regulating the activity of PPM phosphatases.

The crystal chemistry of (Mn3 +, Fe3+)-substituted andalusites (viridines and kanonaite), (Al1−x−yMn3x+Fe3y+)2 (OǀSiO4): crystal structure refinements, Mössbauer, and polarized optical absorption spectra

1981 ◽  
Vol 155 (1-2) ◽  
Author(s):  
I. Abs-Wurmbach ◽  
K. Langer ◽  
F. Seifert ◽  
E. Tillmanns
Keyword(s):  
Crystal Structure ◽  
Transition Metal ◽  
Optical Absorption ◽  
Metal Ions ◽  
Crystal Chemistry ◽  
Mixed Crystal ◽  
Transition Metal Ions ◽  
Structure Type ◽  
Optical Absorption Spectra ◽  
Distorted Octahedral

AbstractThe crystal chemistry of viridines and kanonaite, (AlThe structure refinements reveal that the transition metal ions substitute for Al almost exclusively in the distorted octahedral Al(l) site of the andalusite structure type within the entire mixed crystal series. This is independently proven by the Mössbauer results for

Sign in / Sign up

Export Citation Format

Share Document