Metal Ion Catalysis in Transamination. II. Pyruvate-Glycinate Equilibrium Systems with Some Divalent Metal Ions

1964 ◽  
Vol 86 (22) ◽  
pp. 4846-4850 ◽  
Author(s):  
D. L. Leussing ◽  
D. C. Shultz
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Metal Ion Catalysis

scholarly journals Structure of New Binary and Ternary DNA Polymerase Complexes From Bacteriophage RB69

2021 ◽  
Vol 8 ◽  
Author(s):  
Jongseo Park ◽  
Hyung-Seop Youn ◽  
Jun Yop An ◽  
Youngjin Lee ◽  
Soo Hyun Eom ◽  
...  
Keyword(s):  
Metal Ions ◽  
Dna Polymerase ◽  
Metal Ion ◽  
Ternary Complex ◽  
Critical Role ◽  
Divalent Metal ◽  
Binary Complex ◽  
Divalent Metal Ions ◽  
Divalent Metal Ion ◽  
Initial Binding

DNA polymerase plays a critical role in passing the genetic information of any living organism to its offspring. DNA polymerase from enterobacteria phage RB69 (RB69pol) has both polymerization and exonuclease activities and has been extensively studied as a model system for B-family DNA polymerases. Many binary and ternary complex structures of RB69pol are known, and they all contain a single polymerase-primer/template (P/T) DNA complex. Here, we report a crystal structure of the exonuclease-deficient RB69pol with the P/T duplex in a dimeric form at a resolution of 2.2 Å. The structure includes one new closed ternary complex with a single divalent metal ion bound and one new open binary complex in the pre-insertion state with a vacant dNTP-binding pocket. These complexes suggest that initial binding of the correct dNTP in the open state is much weaker than expected and that initial binding of the second divalent metal ion in the closed state is also much weaker than measured. Additional conformational changes are required to convert these complexes to high-affinity states. Thus, the measured affinities for the correct incoming dNTP and divalent metal ions are average values from many conformationally distinctive states. Our structure provides new insights into the order of the complex assembly involving two divalent metal ions. The biological relevance of specific interactions observed between one RB69pol and the P/T duplex bound to the second RB69pol observed within this dimeric complex is discussed.

scholarly journals Modeling of neotame and fructose thermochemistry: Comparison with mono and divalent metal ions by Computational and experimental approach

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Deepali Sharma ◽  
Suvardhan Kanchi ◽  
Ayyappa Bathinapatla ◽  
Inamuddin ◽  
Abdullah M. Asiri
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Density Functional ◽  
Divalent Metal ◽  
Basis Set ◽  
Hydroxyl Groups ◽  
Specific Cell ◽  
Water Medium ◽  
Artificial Sweetener ◽  
Divalent Metal Ions

AbstractThe metal complexes can demonstrate various interesting biological activities in the human body. However, the role of certain metal ions for specific cell activities is still subject to debate. This study is aimed at comparing the thermochemical properties of neotame (artificial sweetener) and α, β-fructose in gas phase and water medium. The interaction of α and β-fructose, neotame with monovalent and divalent metal ions was studied and comprehended by density functional theory (DFT) using B3LYP functional, 6–311 + G (d, p) and D3 basis set. Metal ion affinities (MIA) values depicted that ionic radius of metal ions played an important role in the interaction of α, β-fructose and neotame. The ∆G parameter was calculated to predict and understand the interaction of metal ions with α and β-fructose, neotame. The results suggested that the presence of hydroxyl groups and oxygen atoms in sugar molecules acted as preferred sites for the binding and interaction of mono and divalent ions. For the first time computational study has been introduced in the present study to review the progress in the application of metal binding with sugar molecules especially with neotame. Moreover, voltammetric behaviour of neotame-Zn2+ was studied using cyclic and differential pulse voltammetry. The obtained results suggest that the peak at −1.13 V is due to the reduction of Zn2+ in 0.1 M phosphate buffer medium at pH 5.5. Whereas, addition of 6-fold higher concentration of neotame to the ZnCl2.2H2O resulted in a new irreversible cathodic peak at −0.83, due to the reduction of neotame-Zn2+ complex. The Fourier transform infrared spectroscopy (FTIR) results indicates that the β-amino group (-NH) and carboxyl carbonyl (-C = O) groups of neotame is participating in the chelation process, which is further supported by DFT studies. The findings of this study identify the efficient chelation factors as major contributors into metal ion affinities, with promising possibilities to determine important biological processes in cell wall and glucose transmembrane transport.

scholarly journals Complementary Metal Ion Specificity of the Metal-Citrate Transporters CitM and CitH of Bacillus subtilis

2000 ◽  
Vol 182 (22) ◽  
pp. 6374-6381 ◽  
Author(s):  
Bastiaan P. Krom ◽  
Jessica B. Warner ◽  
Wil N. Konings ◽  
Juke S. Lolkema
Keyword(s):  
Bacillus Subtilis ◽  
Metal Ions ◽  
Metal Ion ◽  
Physiological Function ◽  
Divalent Metal ◽  
Uptake System ◽  
Divalent Metal Ions ◽  
Ion Specificity ◽  
Citrate Transporter ◽  
Wide Range

ABSTRACT Citrate uptake in Bacillus subtilis is stimulated by a wide range of divalent metal ions. The metal ions were separated into two groups based on the expression pattern of the uptake system. The two groups correlated with the metal ion specificity of two homologousB. subtilis secondary citrate transporters, CitM and CitH, upon expression in Escherichia coli. CitM transported citrate in complex with Mg2+, Ni2+, Mn2+, Co2+, and Zn2+ but not in complex with Ca2+, Ba2+, and Sr2+. CitH transported citrate in complex with Ca2+, Ba2+, and Sr2+ but not in complex with Mg2+, Ni2+, Mn2+, Co2+, and Zn2+. Both transporters did not transport free citrate. Nevertheless, free citrate uptake could be demonstrated in B. subtilis, indicating the expression of at least a third citrate transporter, whose identity is not known. For both the CitM and CitH transporters it was demonstrated that the metal ion promoted citrate uptake and, vice versa, that citrate promoted uptake of the metal ion, indicating that the complex is the transported species. The results indicate that CitM and CitH are secondary transporters that transport complexes of divalent metal ions and citrate but with a complementary metal ion specificity. The potential physiological function of the two transporters is discussed.

Divalent metal ion-mediated assembly of spherical nucleic acids: the case study of Cu2+

2015 ◽  
Vol 17 (45) ◽  
pp. 30292-30299 ◽  
Author(s):  
Jang Ho Joo ◽  
Jae-Seung Lee
Keyword(s):  
Nucleic Acids ◽  
Metal Ions ◽  
Metal Ion ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
New Strategy ◽  
Divalent Metal Ion ◽  
Spherical Nucleic Acids

A new strategy for reversibly assembling spherical nucleic acids (SNAs) is demonstrated based on the coordinative binding of divalent metal ions, particularly Cu2+, to nucleobases.

scholarly journals Effect of divalent metal ions on annexin-mediated aggregation of asolectin liposomes.

2000 ◽  
Vol 47 (3) ◽  
pp. 675-683 ◽  
Author(s):  
V I Mel'gunov ◽  
E I Akimova ◽  
K S Krasavchenko
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Relative Concentration ◽  
Toxic Metal ◽  
Transition Metal Ions ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Large Unilamellar Vesicles ◽  
Protein Molecules ◽  
Divalent Metal Ion

Annexins belong to a family of Ca2+- and phospholipid-binding proteins that can mediate the aggregation of granules and vesicles in the presence of Ca2+. We have studied the effects of different divalent metal ions on annexin-mediated aggregation of liposomes using annexins isolated from rabbit liver and large unilamellar vesicles prepared from soybean asolectin II-S. In the course of these studies, we have found that annexin-mediated aggregation of liposomes can be driven by various earth and transition metal ions other than Ca2+. The ability of metal ions to induce annexin-mediated aggregation decreases in the order: Cd2+ > Ba2+, Sr2+ > Ca2+ > Mn2+ > Ni2+ > Co2+. Annexin-mediated aggregation of vesicles is more selective to metal ions than the binding of annexins to membranes. We speculate that not every type of divalent metal ion can induce conformational change sufficient to promote the interaction of annexins either with two opposing membranes or with opposing protein molecules. Relative concentration ratios of metal ions in the intimate environment may be crucial for the functioning of annexins within specialized tissues and after treatment with toxic metal ions.

Alginate Polyelectrolyte Ionotropic Gels-XII. Chromatographic Separation of Divalent Transition Metal Ions using Alginates as Ion Exchangers

1992 ◽  
Vol 4 (1) ◽  
pp. 49-54 ◽  
Author(s):  
Refat M. Hassan ◽  
S. A. El-Shatoury ◽  
M. Th. Makhlouf
Keyword(s):  
Ion Exchange ◽  
Metal Ions ◽  
Metal Ion ◽  
Transition Metal Ions ◽  
Selectivity Coefficient ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Ion Exchangers ◽  
Calcium Alginate Gel ◽  
Exchange Selectivity

The separation of divalent metal ion mixtures has been investigated chromatographically on columns of either gel or sol forms of alginate polyelectrolyte. Separation was obtained in the form of narrow sharp zones for the metal ions. Ion exchange selectivity indicated that Cu2+ ions were most strongly retained among the divalent metal ions studied. The factors which affect the ion exchange selectivity, such as the strength of chelation and the mobility and radii of the metal ions, are discussed. The selectivity coefficient for the separation of a mixture of Cu2+ and Co2+ ions on columns of calcium alginate gel or sodium alginate sol was determined and found to be 1.9 ± 0.1 in both ion exchangers at 25°C.

scholarly journals Long-Chain Polyphosphate Causes Cell Lysis and Inhibits Bacillus cereus Septum Formation, Which Is Dependent on Divalent Cations

1999 ◽  
Vol 65 (9) ◽  
pp. 3942-3949 ◽  
Author(s):  
Simon K. Maier ◽  
Siegfried Scherer ◽  
Martin J. Loessner
Keyword(s):  
Cell Division ◽  
Metal Ions ◽  
Bacillus Cereus ◽  
Metal Ion ◽  
Divalent Cations ◽  
Divalent Metal ◽  
Divalent Metal Ions ◽  
Septum Formation ◽  
Cell Counts ◽  
Long Chain

ABSTRACT We investigated the cellular mechanisms that led to growth inhibition, morphological changes, and lysis of Bacillus cereus WSBC 10030 when it was challenged with a long-chain polyphosphate (polyP). At a concentration of 0.1% or higher, polyP had a bacteriocidal effect on log-phase cells, in which it induced rapid lysis and reductions in viable cell counts of up to 3 log units. The cellular debris consisted of empty cell wall cylinders and polar caps, suggesting that polyP-induced lysis was spatially specific. This activity was strictly dependent on active growth and cell division, since polyP failed to induce lysis in cells treated with chloramphenicol and in stationary-phase cells, which were, however, bacteriostatically inhibited by polyP. Similar observations were made with B. cereus spores; 0.1% polyP inhibited spore germination and outgrowth, and a higher concentration (1.0%) was even sporocidal. Supplemental divalent metal ions (Mg2+ and Ca2+) could almost completely block and reverse the antimicrobial activity of polyP; i.e., they could immediately stop lysis and reinitiate rapid cell division and multiplication. Interestingly, a sublethal polyP concentration (0.05%) led to the formation of elongated cells (average length, 70 μm) after 4 h of incubation. While DNA replication and chromosome segregation were undisturbed, electron microscopy revealed a complete lack of septum formation within the filaments. Exposure to divalent cations resulted in instantaneous formation and growth of ring-shaped edges of invaginating septal walls. After approximately 30 min, septation was complete, and cell division resumed. We frequently observed a minicell-like phenotype and other septation defects, which were probably due to hyperdivision activity after cation supplementation. We propose that polyP may have an effect on the ubiquitous bacterial cell division protein FtsZ, whose GTPase activity is known to be strictly dependent on divalent metal ions. It is tempting to speculate that polyP, because of its metal ion-chelating nature, indirectly blocks the dynamic formation (polymerization) of the Z ring, which would explain the aseptate phenotype.

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