• Title/Summary/Keyword: Divalent ions

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Stability Constants of Divalent Transition and Trivalent Lanthanide Metal Ion Complexes of Macrocyclic Triazatri(Methylacetic Acid)

  • 김동원;홍춘표;최기영;김창숙;이남수;장영훈;이재국
    • Bulletin of the Korean Chemical Society
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    • v.17 no.9
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    • pp.790-793
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    • 1996
  • The azacrown compound, 1,7-dioxa-4,10,13-triazacyclopentadecane-N,N',N"-tri(methyl-acetic acid)(N3O2-tri(methylacetic acid)) was synthesized by modified procedure of Krespan. Potentiometric method has been used to determine the protonation constants of N3O2-tri(methylacetic acid) and stability constants of complexes on the divalent transition metal ions (Co2+, Ni2+, Cu2+, and Zn2+) and trivalent metal ions (Ce3+, Eu3+, Gd3+, and Yb3+) with N3O2-tri(methylacetic acid). The stability constants for the complexes of the divalent transition metal ions studied in the present work with N3O2-tri(methylacetic acid) were 11.4 for Co2+, 11.63 for Ni2+, 13.51 for Cu2+, and 11.65 for Zn2+, respectively. Thus, the order of the stability constants for complexes on the transition metal ions with N3O2-tri(methylacetic acid) was shown Co2+ < Ni2+ < Cu2+ > Zn2+ as same as the order of Irving-Williams series. The stability constants of Ce3+, Eu3+, Gd3+, and Yb3+ trivalent lanthanide metal ion complexes of N3O2-tri(methylacetic acid) were, respectively, 11.26 for Ce3+, 11.56 for Eu3+, 11.49 for Gd3+, and 11.80 for Yb3+. The values of the stability constants on trivalent metal ions with the ligand are increasing according to increase atomic number, due to increase acidity. But the value of stability constant of Gd3+ ion is less than the value of Eu3+ ion. This disordered behavior is also reported by Moeller.

Effects of various metal ions on the gene expression of iron exporter ferroportin-l in J774 macrophages

  • Park, Bo-Yeon;Chung, Ja-Yong
    • Nutrition Research and Practice
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    • v.2 no.4
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    • pp.317-321
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    • 2008
  • Macrophages play a key role in iron metabolism by recycling iron through erythrophagocytosis. Ferroportin-l (FPN1) is a transporter protein that is known to mediate iron export from macrophages. Since divalent metals often interact with iron metabolism, we examined if divalent metals could regulate the expression of FPN1 in macrophages. J774 macrophage cells were treated with copper, manganese, zinc, or cobalt at 10, 50, or $100\;{\mu}M$ for 16 to 24 h. Then, FPN1 mRNA and protein levels were determined by quantitative real-time PCR and Western blot analyses, respectively. In addition, effects of divalent metals on FPN1 promoter activity were examined by luciferase reporter assays. Results showed that copper significantly increased FPN1 mRNA levels in a dose-dependent manner. The copper-induced expression of FPN1 mRNA was associated with a corresponding increase in FPN1 protein levels. Also, copper directly stimulated the activity of FPN1 promoter-driven reporter construct. In contrast, manganese and zinc had no effect on the FPN1 gene expression in J774 cells. Interestingly, cobalt treatment in J774 cells decreased FPN1 protein levels without affecting FPN1 mRNA levels. In conclusion, our study results demonstrate that divalent metals differentially regulate FPN1 expression in macrophages and indicate a potential interaction of divalent metals with the FPN1-mediated iron export in macrophages.

Purification and properties of polyphosphate phosphohydrolase from chlorella ellipsoidea (Chlorellaellipsoidea로 부터 polyphosphate phosphohydrolase의 분리, 정제 및 성질)

  • 임영복;이영록
    • Korean Journal of Microbiology
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    • v.21 no.3
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    • pp.135-142
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    • 1983
  • The presence of polyphosphate phosphohydrolase (PPPH) and tripolyphosphate phosphohydrolase (TPPH) in Chlorella ellipsoidea were confirmed from the cell-free extract of the algal cells and three forms of PPPH were isolated, purified, and measured Km-Vmax value and inhibitory effect by metal ions, respectively. PPPH was most active at pH7.2, whereas TPPH at pH 7.6. Both enzymes exhibited their maximum activity at $37^{\circ}C$. For the manifestation of catalytic activity, divalent, divalent metal ions are needed, and the best activator for both enzymes was $Co^{++}\;ions\;(10^{-3}M)$. These enzymes were inhibited by $Hg^{++}\;ions\;(10^{-3}M)$ considerably. PPPH from Chlorella ellipsoidea was purified by ammonium sulfate fractionation, ion-exchange chromatography on DEAE-Sephadex A-25, and gel filtration on Sephadex G-100, and some properties of the three different fraction with PPPH activity $(PPPH_1,\;PPPH_2,\;and\;PPPH_3)$ were found, i.e, PPPH has multiple form. The Km values of $PPPH_1,\;PPPH_2,\;and\;PPPH_3$ obstained were $6.25{\times}10^{-4}M,\;10^{-4}M-4/M,\;and\;3.33{times}10^{-4}M$ and Vmax were 3.33 mM/min, 3.33 mM/min, and 2.67 mM/min, respectively. It was shown that the types of inhibition of $Hg^{++} on the activities of three forms of PPPH were competitive inhibition.

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XMCD and PES study of a compensated-ferrimagnetic half-metal Mn3Ga

  • Seong, Seungho;Lee, Eunsook;Kim, Hee Yeon;Kim, Younghak;Baik, Jaeyoon;Kang, J.S.
    • Current Applied Physics
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    • v.18 no.11
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    • pp.1190-1195
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    • 2018
  • By employing soft X-ray magnetic circular dichroism (XMCD), soft X-ray absorption spectroscopy (XAS), and photoemission spectroscopy (PES), we have investigated the electronic structure of the candidate zero-moment half-metallic $Mn_3Ga$. We have studied the ball-milled and annealed $Mn_3Ga$ powder samples that exhibit nearly zero magnetization. Mn 2p XAS revealed that Mn ions in $Mn_3Ga$ are nearly divalent for both of the Mn ions having the locally octahedral symmetry and those having the locally tetrahedral symmetry. The measured Mn 2p XMCD spectrum of $Mn_3Ga$ is very similar to that of ferrimagnetic $MnFe_2O_4$ having divalent Mn ions. The sum-rule analysis of the Mn 2p XMCD spectrum shows that both the spin and orbital magnetic moments of Mn ions in $Mn_3Ga$ are negligibly small, in agreement with the nearly compensated-ferrimagnetic ground state of $Mn_3Ga$. The valence-band PES spectrum of $Mn_3Ga$ agrees well with the calculated density of states, supporting the half-metallic electronic structure of $Mn_3Ga$.

Effects of ATP and ADP on iron uptake in rat heart mitochondria

  • Kim, Mi-Sun;Song, Eun-Sook
    • Animal cells and systems
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    • v.14 no.4
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    • pp.245-252
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    • 2010
  • Iron uptake in mitochondria and fractionated mitochondria compartments was studied to understand iron transport in heart mitochondria. The inner membrane is most active in iron uptake. Mitochondrial uptake was dependent on iron concentration and the amount of mitochondria. Iron transport was inversely proportional to pH in the range of 6.0 to 8.0. Iron transport reached a maximum after 30 min of incubation at $37^{\circ}C$. Iron uptake was inhibited by 1 mM ATP and stimulated by 1 mM ADP. The oxidative phosphorylation inhibitor oligomycin inhibited iron uptake, but rotenone and antimycin A did not. The divalent ions $Mg^{2+}$, $Cu^{2+}$, $Mn^{2+}$, and $Zn^{2+}$ suppressed iron uptake at $10\;{\mu}M$ and stimulated it at 1 mM. The divalent ion $Ca^{2+}$ stimulated iron uptake at $10\;{\mu}M$ and suppressed it at 1 mM, competing with iron. The uptake of calcium was stimulated by 10 to $1000\;{\mu}M$ ATP, while iron uptake was stimulated reciprocally by 10 to $1000\;{\mu}M$ ADP, suggesting that these ions have movements similar to those of ATP and ADP.

Physicochemical Properties of Protoporphyrin IX by Metal Ions in Acetonitrile-Water Mixture Solution

  • Bark, Ki-Min;Yang, Jeong-Im;Lee, Ho-Suk;Lee, Jee-Bum;Park, Chul-Ho;Park, Hyoung-Ryun
    • Bulletin of the Korean Chemical Society
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    • v.31 no.6
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    • pp.1633-1637
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    • 2010
  • The UV-vis absorption spectrum of protoporphyrin IX shows a very sharp and strong absorption maximum peak at 398 nm in acetonitrile-water mixture solution (1:1 v/v). When divalent metal ions such as $Cu^{2+}$, $Zn^{2+}$, and $Ca^{2+}$ ion were added to protoporphyrin IX, metal protoporphyrin IX complexes were thereby produced. Cu-protoporphyrin IX complexes have the largest formation constant ($K_f$) among them. The fluorescence intensity of protoporphyrin IX was diminished by the presence of $Cu^{2+}$, $Zn^{2+}$, $Ca^{2+}$, $Mn^{2+}$, and $Ni^{2+}$ ions as quenchers. However, $Mg^{2+}$, $Mn^{2+}$, and $Ni^{2+}$ ions are hardly combined with protoporphyrin IX. $Mg^{2+}$ ion does not take part in the fluorescence quenching process of protoporphyrin IX in acetonitrile-water mixture solution. According to the Stern-Volmer plots, fluorescence quenching by $Cu^{2+}$, $Zn^{2+}$, and $Ca^{2+}$ ions involves static quenching, which is due to complex formation. On the contrary, dynamic quenching has a large influence on the overall quenching process, when $Mn^{2+}$ and $Ni^{2+}$ ions were added to protoporphyrin IX in acetonitrile-water mixture solution.

Evaluation of the Effective Charge Density on Low Pressure Nanofiltration with the Separation Characteristics of Monovalent and Divalent Solutes in the Production of Drinking Water

  • Oh, Jeong-Ik;Taro, Urase
    • Environmental Engineering Research
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    • v.16 no.1
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    • pp.29-34
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    • 2011
  • The electric charge on a membrane was investigated by analyzing the experimental rejection of various monovalent and divalent ionic solutes. The characteristics of the separation of ionic solutes using various nanofiltration membranes were obtained from an experimental nanofiltration set-up, with a surface area of $40cm^2$ under the operational pressures between 0.25-0.3 MPa. The state of the membrane electric charge was observed using separation coefficients, i.e., the permeation ratio of monovalent to divalent ions. To confirm the state of the membrane charge observed via the separation coefficient, a calculation using the extended Nernst-Planck equation, coupled with the Donnan equilibrium, assuming different electric charge states of the membrane, was compared with the experimental rejection of ionic solutes. The examination of the characteristics of separation using three types of nanofiltration membranes showed that one of the membranes carried a negative/positive double charge density inside, while other two membranes carried either a positive or negative charge density.

Importance of Cytochrome P450 3A4 Conformation for the Activity Stimulation by Cytochrome b5 : Specific Inhibition of Cytochrome P450 3A4 by Zinc (II) Ion

  • Kim, Joon-Sik;Yun, Chul-Ho
    • Proceedings of the PSK Conference
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    • 2003.04a
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    • pp.149.3-150
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    • 2003
  • CYP3A4 is the most abundant human CYP and oxidizes a diversity of substrates. including various drugs. steroids. and carcinogens. A variety of metal ions are known to affect microsomal monooxygenase activities. Effects of a series of divalent metal ions on the CYP3A4-catalyzed reaction of reconstituted system containing purified CYP3A4. NADPH-P450 reductase (NPR), and cytochrome b5 (b5) were examined. (omitted)

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Electronic structure studies of CoFeRO (R=Hf,La,Nb) thin films by X-ray absorption spectroscopy

  • Song, J.H.;Gautam, S.;Chae, K.H.;Asokan, K.
    • Proceedings of the Korean Vacuum Society Conference
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    • 2010.02a
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    • pp.378-378
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    • 2010
  • We report the electronic structure of CoFeO-R (R=Hf, La, Nb) thin films studied by x-ray absorption spectroscopy (XAS). These ferrites thin films were prepared by pulsed laser deposition method and characterized by XAS measurements at O K-, Co and Fe L-edges. The O K-edge spectra suggest that there is a strong hybridization between O 2p and 3d electrons of transition metal cations and Fe $L_{3,2}$-edge spectra indicate that Fe-ions exist in $Fe^{2+}$ with tetrahedral site of the spinel structure. Divalent Co ions is also distributed in tetrahedral site with rare earth ions goes to octahedral sites of spinel structure. X-ray magnetic circular dichroism (XMCD) is also used to explain the symmetry and magnetic nature dependence on rare-earth ions.

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