scholarly journals Biosorption of Microelements bySpirulina: Towards Technology of Mineral Feed Supplements

2014 ◽  
Vol 2014 ◽  
pp. 1-15 ◽  
Author(s):  
Agnieszka Dmytryk ◽  
Agnieszka Saeid ◽  
Katarzyna Chojnacka
Keyword(s):  
Metal Ions ◽  
Potentiometric Titration ◽  
Metal Ion ◽  
Surface Characterization ◽  
Multicomponent Systems ◽  
Icp Oes ◽  
Metal Ion Binding ◽  
Metal Ion Adsorption ◽  
Loaded Material ◽  
Titration Data

Surface characterization and metal ion adsorption properties ofSpirulinasp. andSpirulina maximawere verified by various instrumental techniques. FTIR spectroscopy and potentiometric titration were used for qualitative and quantitative determination of metal ion-binding groups. Comparative FTIR spectra of natural and Cu(II)-treated biomass proved involvement of both phosphoryl and sulfone groups in metal ions sorption. The potentiometric titration data analysis provided the best fit with the model assuming the presence of three types of surface functional groups and the carboxyl group as the major binding site. The mechanism of metal ions biosorption was investigated by comparing the results from multielemental analyses by ICP-OES and SEM-EDX. Biosorption of Cu(II), Mn(II), Zn(II), and Co(II) ions by lyophilizedSpirulinasp. was performed to determine the metal affinity relationships for single- and multicomponent systems. Obtained results showed the replacement of naturally bound ions: Na(I), K(I), or Ca(II) with sorbed metal ions in a descending order of Mn(II) > Cu(II) > Zn(II) > Co(II) for single- and Cu(II) > Mn(II) > Co(II) > Zn(II) for multicomponent systems, respectively. Surface elemental composition of natural and metal-loaded material was determined both by ICP-OES and SEM-EDX analysis, showing relatively high value of correlation coefficient between the concentration of Na(I) ions in algal biomass.

The influence of metal-ion binding on the structure and surface composition of Sonic Hedgehog: a combined classical and hybrid QM/MM MD study

2016 ◽  
Vol 18 (32) ◽  
pp. 22254-22265 ◽  
Author(s):  
Manuel Hitzenberger ◽  
Thomas S. Hofer
Keyword(s):  
Metal Ions ◽  
Sonic Hedgehog ◽  
Binding Sites ◽  
Metal Ion ◽  
Surface Composition ◽  
Quantum Mechanical ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Structural Impact

The interaction of metal ions with Shh binding-sites and their structural impact are assessed via classical and quantum mechanical simulations.

scholarly journals Functional characterization of the dimerization domain of the ferric uptake regulator (Fur) of Pseudomonas aeruginosa

2006 ◽  
Vol 400 (3) ◽  
pp. 385-392 ◽  
Author(s):  
Erdeni Bai ◽  
Federico I. Rosell ◽  
Bao Lige ◽  
Marcia R. Mauk ◽  
Barbara Lelj-Garolla ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Metal Ions ◽  
Binding Site ◽  
Metal Ion ◽  
Association Constants ◽  
Ion Binding ◽  
Ferric Uptake Regulator ◽  
Metal Ion Binding ◽  
Dimerization Domain ◽  
High Affinity

The functional properties of the recombinant C-terminal dimerization domain of the Pseudomonas aeruginosa Fur (ferric uptake regulator) protein expressed in and purified from Escherichia coli have been evaluated. Sedimentation velocity measurements demonstrate that this domain is dimeric, and the UV CD spectrum is consistent with a secondary structure similar to that observed for the corresponding region of the crystallographically characterized wild-type protein. The thermal stability of the domain as determined by CD spectroscopy decreases significantly as pH is increased and increases significantly as metal ions are added. Potentiometric titrations (pH 6.5) establish that the domain possesses a high-affinity and a low-affinity binding site for metal ions. The high-affinity (sensory) binding site demonstrates association constants (KA) of 10(±7)×106, 5.7(±3)×106, 2.0(±2)×106 and 2.0(±3)×104 M−1 for Ni2+, Zn2+, Co2+ and Mn2+ respectively, while the low-affinity (structural) site exhibits association constants of 1.3(±2)×106, 3.2(±2)×104, 1.76(±1)×105 and 1.5(±2)×103 M−1 respectively for the same metal ions (pH 6.5, 300 mM NaCl, 25 °C). The stability of metal ion binding to the sensory site follows the Irving–Williams order, while metal ion binding to the partial sensory site present in the domain does not. Fluorescence experiments indicate that the quenching resulting from binding of Co2+ is reversed by subsequent titration with Zn2+. We conclude that the domain is a reasonable model for many properties of the full-length protein and is amenable to some analyses that the limited solubility of the full-length protein prevents.

scholarly journals Crystallographic and X-ray absorption spectroscopic characterization of Helicobacter pylori UreE bound to Ni2+ and Zn2+ reveals a role for the disordered C-terminal arm in metal trafficking

2012 ◽  
Vol 441 (3) ◽  
pp. 1017-1035 ◽  
Author(s):  
Katarzyna Banaszak ◽  
Vlad Martin-Diaconescu ◽  
Matteo Bellucci ◽  
Barbara Zambelli ◽  
Wojciech Rypniewski ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Metal Ions ◽  
Metal Binding ◽  
Metal Ion ◽  
Mutual Influence ◽  
Accurate Information ◽  
Metal Ion Binding ◽  
X Ray ◽  
X Ray Absorption

The survival and growth of the pathogen Helicobacter pylori in the gastric acidic environment is ensured by the activity of urease, an enzyme containing two essential Ni2+ ions in the active site. The metallo-chaperone UreE facilitates in vivo Ni2+ insertion into the apoenzyme. Crystals of apo-HpUreE (H. pylori UreE) and its Ni2+- and Zn2+-bound forms were obtained from protein solutions in the absence and presence of the metal ions. The crystal structures of the homodimeric protein, determined at 2.00 Å (apo), 1.59 Å (Ni2+) and 2.52 Å (Zn2+) resolution, show the conserved proximal and solvent-exposed His102 residues from two adjacent monomers invariably involved in metal binding. The C-terminal regions of the apoprotein are disordered in the crystal, but acquire significant ordering in the presence of the metal ions due to the binding of His152. The analysis of X-ray absorption spectral data obtained using solutions of Ni2+- and Zn2+-bound HpUreE provided accurate information of the metal-ion environment in the absence of solid-state effects. These results reveal the role of the histidine residues at the protein C-terminus in metal-ion binding, and the mutual influence of protein framework and metal-ion stereo-electronic properties in establishing co-ordination number and geometry leading to metal selectivity.

Bromine substituted aminonaphthoquinones: synthesis, characterization, DFT and metal ion binding studies

RSC Advances ◽  
2016 ◽  
Vol 6 (91) ◽  
pp. 88010-88029 ◽  
Author(s):  
Gunjan Agarwal ◽  
Dipali N. Lande ◽  
Debamitra Chakrovarty ◽  
Shridhar P. Gejji ◽  
Prajakta Gosavi-Mirkute ◽  
...  
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Binding Studies

Bromine substituted aminonaphthoquinones – chemosensors for metal ions.

Functional group effect of isoreticular metal–organic frameworks on heavy metal ion adsorption

2018 ◽  
Vol 42 (11) ◽  
pp. 8864-8873 ◽  
Author(s):  
Leili Esrafili ◽  
Vahid Safarifard ◽  
Elham Tahmasebi ◽  
M. D. Esrafili ◽  
Ali Morsali
Keyword(s):  
Heavy Metal ◽  
Metal Ions ◽  
Metal Ion ◽  
Heavy Metal Ions ◽  
Functional Group ◽  
Metal Organic Frameworks ◽  
Ion Adsorption ◽  
Group Effect ◽  
Metal Ion Adsorption ◽  
Metal Organic

We examined adsorption behavior of some MOFs having different functional groups in their pillar structures for adsorption of some heavy metal ions.

scholarly journals Removal of heavy metal ions from wastewater by capacitive deionization using polypyrrole/chitosan composite electrode

2019 ◽  
Vol 37 (3-4) ◽  
pp. 205-216 ◽  
Author(s):  
Yujie Zhang ◽  
Quanqin Xue ◽  
Fei Li ◽  
Jizhe Dai
Keyword(s):  
Heavy Metal ◽  
Composite Material ◽  
Metal Ions ◽  
Metal Ion ◽  
Heavy Metal Ions ◽  
Composite Electrode ◽  
Capacitive Deionization ◽  
Metal Ion Adsorption ◽  
Adsorption Desorption ◽  
Chitosan Composite

A polypyrrole/chitosan composite material was obtained by chemical polymerization. The adsorption performance of a hot-molded polypyrrole/chitosan composite electrode was tested by adsorption/desorption experiments. Scanning electron microscopy and Fourier-transform infrared spectroscopy both showed the deposition of polypyrrole on the chitosan surface. The specific capacitance of the polypyrrole/chitosan composite was determined by cyclic voltammetry in 1.0 M KCl at 0.01 V/s as 102.96 F/g. The adsorption/desorption experiments indicated that the specific adsorption capacity of the composite for Cu2+ was 99.67 mg/g, while the removal performance for other metal ions, such as Ag+, Pb2+, and Cd2+, was good. The results of multicycle adsorption/desorption tests showed that the adsorption rate of the polypyrrole/chitosan composite electrode for Cu2+ was decreased from 56.4 to 51.4% over 10 cycles, demonstrating the stable metal-ion adsorption/desorption behavior of the composite electrode. The obtained performances show that the prepared polypyrrole/chitosan composite material is an ideal electrode material for the removal of heavy metal ions.

New multidentate ligands. XXI. Synthesis, proton, and metal ion binding affinities of N,N′,N″-tris[2-(N-hydroxycarbamoyl)ethyl]-1,3,5-benzenetricarboxamide (BAMTPH)

1983 ◽  
Vol 61 (12) ◽  
pp. 2740-2744 ◽  
Author(s):  
Isao Yoshida ◽  
Ichiro Murase ◽  
Ramunas J. Motekaitis ◽  
Arthur E. Martell
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Binding Constants ◽  
Cation Binding ◽  
Ion Binding ◽  
Binding Affinities ◽  
Metal Ion Binding ◽  
Trivalent Metal ◽  
Equilibrium Data ◽  
Trivalent Metal Ions

Synthesis of a new tris-bidentate multidentate ligand, N,N′,N″-tris[2-(N-hydroxycarbamoyl)ethyl]-1,3,5-benzenetricarboxamide (BAMTPH), designed for the binding of trivalent metal ions such as Fe(III), Ga(III), and Al(III), is described. Its cation binding affinities for hydrogen ion and for Fe(III), Co(II), Ni(II), Cu(II), Zn(II), Ga(III), and Al(III) ions are described, and the equilibrium data are compared with those of analogous ligands. The binding constants of trivalent metal ions with the ligand do not show a chelate effect relative to the binding to individual bidentate hydroxamic acids.

scholarly journals Computational approaches for de novo design and redesign of metal-binding sites on proteins

2017 ◽  
Vol 37 (2) ◽  
Author(s):  
Gunseli Bayram Akcapinar ◽  
Osman Ugur Sezerman
Keyword(s):  
Metal Ions ◽  
Metal Binding ◽  
Binding Sites ◽  
Metal Ion ◽  
De Novo ◽  
De Novo Design ◽  
Ion Binding ◽  
Chemical Transformations ◽  
Metal Ion Binding ◽  
Metal Binding Sites

Metal ions play pivotal roles in protein structure, function and stability. The functional and structural diversity of proteins in nature expanded with the incorporation of metal ions or clusters in proteins. Approximately one-third of these proteins in the databases contain metal ions. Many biological and chemical processes in nature involve metal ion-binding proteins, aka metalloproteins. Many cellular reactions that underpin life require metalloproteins. Most of the remarkable, complex chemical transformations are catalysed by metalloenzymes. Realization of the importance of metal-binding sites in a variety of cellular events led to the advancement of various computational methods for their prediction and characterization. Furthermore, as structural and functional knowledgebase about metalloproteins is expanding with advances in computational and experimental fields, the focus of the research is now shifting towards de novo design and redesign of metalloproteins to extend nature’s own diversity beyond its limits. In this review, we will focus on the computational toolbox for prediction of metal ion-binding sites, de novo metalloprotein design and redesign. We will also give examples of tailor-made artificial metalloproteins designed with the computational toolbox.

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