• 한국환경농학회지
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• 제17권3호
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• pp.246-253
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• 1998

광산폐수, 산업폐수등으로 부터 Cd, Pb, Zn 및 Cu 등의 중금속에 강한 내성을 지니고 있을 뿐만 아니라 균체내 중금속 축적능력이 우수한 중금속 내성 미생물 균주 Pseudomonas putida, P. aeruginosa, P. chlororaphis 및 P. stutzeri를 각각 분리하여, 화학적인 방법으로 세포내 functional group들의 전하를 인위적으로 변형시켜 변형시키기 전과의 중금속 결합능력을 비교 조사한 결과는 다음과 같다. 화학적인 방법으로 functional group의 charge를 변형시킨 cell wall들에 의한 중금속 축적변화를 조사한 결과, cell wall중 amine group을 변형시켰을 경우에는 중금속 축적율이 변형시키지 않은 cell wall에 비하여 약간 증가되었거나 거의 비슷한 축적율을 나타내었으나, carboxyl group을 변형시켰을 경우에는 매우 크게 감소되었다. 이와같은 결과는 functional group을 변형시킨 cell wall의 외형적인 중금속 축적형태를 전자현미경으로 관찰하였을 경우에도 명확하게 나타났으며, 따라서, carboxyl기는 중요한 중금속 binding site인 것으로 판단되었다.

• 한국자기공명학회논문지
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• 제19권2호
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• pp.67-73
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• 2015

The microcystin is a cyclic heptapeptide from metabolites of cyanobacteria in the genera mycrocystis, anabaeba as a result of eutrophication. It has been known that microcystin-LR is a potent inhibitor of the catalytic subunits of protein phosphatase-1 (PP-1) as well as powerful tumor promoter. The active site of microcystin actually has two metal ions $Fe^{2+}/Zn^{2+}$ close to the nucleophilic portion of PP-1-microcystin complex. We report the isolation and purification of this microcystin-LR from cyanobacteria (blue-green algae) obtained from Daechung Dam in Chung-cheong Do, Korea. Microcystin-LR was extracted from solid-phase extraction (SPE) sample preparation using a CN cartridge. The cyanobacteria extract was purified to obtain microcystin-LR by HPLC method and identified by LC/MS. The detail structural studies that can elucidate the possible role of monovalent and divalent metal ions in PP-1-microcystin complexation were carried out by utilizing molecular dynamics. Conformational changes in metal binding for ligands were monitored by molecular dynamic computation and potential of mean force (PMF) using the method of the free energy perturbation. The microcystin-metal binding PMF simulation results exhibit that microcystin can have very stable binding free energy of -10.95 kcal/mol by adopting the $Mg^{2+}$ ion at broad geometrical distribution of $0.5{\sim}4.5{\AA}$, and show that the $K^+$ ion can form a stable metal complex rather than other monovalent alkali metal ions.

• Bulletin of the Korean Chemical Society
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• 제30권9호
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• pp.1996-2000
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• 2009

Alkali metal salts were introduced to enhance the ionization efficiency of glucose and maltooligoses in electrospray ionization-mass spectrometry (ESI-MS). A mixture of the same moles of glucose, maltose, maltotriose, maltotetraose, maltopentaose, maltohexaose, and maltoheptaose was used. Salts of lithium, sodium, potassium, and cesium were employed as the cationizing agent. The ionization efficiency varied with the alkali metal cation types as well as the analyte sizes. Ion abundance distribution of the [M+$cation]^+$ ions of the carbohydrates varied with the fragmentor voltage. The maximum ion abundance at low fragmentor voltage was observed at maltose, while the maximum ion abundance at high fragmentor voltage shifted to maltotriose or maltotetraose for Na, K, and Cs. Variation of the ionization efficiency was explained with the hydrated cation size and the binding energy of the analyte and alkali metal cation.

• Bulletin of the Korean Chemical Society
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• 제35권4호
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• pp.1087-1090
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• 2014

A simple and general method that selectively introduces metal binding sites into a protein can greatly increase the ability to design and biosynthesize artificial metalloproteins. Here, we report the incorporation of a phenanthroline-containing amino acid (Phen-Ala) into proteins in Escherichia coli by using the $tRNA{^{Tyr}}_{CUA}$ and tyrosyl aminoacyl-tRNA synthetase pair (BpyRS) from Methanococcus jannaschii, which was originally developed for a bipyridine-containing amino acid (Bpy-Ala). The incorporation efficiency of BpyRS for Phen-Ala was comparable to that for Bpy-Ala. Because of its high metal-binding ability and characteristic spectral properties, Phen-Ala can be a useful alternative to the existing metal-chelating amino acids for the design and synthesis of artificial metalloproteins.

• The Korean Journal of Ecology
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• 제19권6호
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• pp.519-527
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• 1996

To examine the possibility of biomonitoring of heavy metal removal ability and soil, a study was performed to investigate the heavy metal removal ability and metal-binding protein (MBP) as detoxification process using Oenanthe stolonifera. After O. stolonifera was exposed to individuals (cadmium, zinc) and mixture (cadmium+zinc)for 4 days, removal rate of heavy metal and pH in the treatment medium was measured. MBP was assayed by means of ion exchange column chromatography. The exposure to mixture (Cd:76.8%, Zn:75%) rather than individuals (Cd:82.9%, Zn:90.4%) showed a synergism raising the toxic effect. Initial removal rate was different for each heavy metal : in case of exposure to cadmium it was over 60% on day 1, while for zinc it was 75~90% on day 4. Throughout the experimental period, pH value of treatment medium continuously decreased, since cortex in the roots may secret organic acid to adjust and prevent toxicity of metals. The existence or MBP in the 70~80 fraction and the presence of Zn-enzyme pool was ascertained with the column chromatography. This study demonstrated a possibility that heavy utilized as a biomarker of heavy metal pollution.

• 대한화학회지
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• 제37권5호
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• pp.491-495
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• 1993

고분자물질로 지지된 아자크라운 에테르(polymer supported azacrown ether:DBPDA ion exchanger)를 합성하고, 이 이온교환체와 Li, Na, 그리고 K의 피크레이트염과의 이온결합등에 대하여 알아보았다. 그리고, DBPDA 이온교환체와 알칼리 피크린산염의 에테르형 용매내에서 알칼리 금속이온들의 결합상수(binding constant:Kb)를 분광광도법을 통하여 구하였다. 그 결과, 결합상수의 크기는 Li < Na < K 순으로 증가하였으며, 리간드와 1:1 착물을 형성한다는 것을 알 수 있었다. 또한 이들의 Kb값들은 용매 및 온도 등과 같은 것들에 의하여 변화하였으며, 그 값들은 $2{\times}10^3{\sim}4{\times}10^4M^{-1}$ 범위내에 있었다. 한편 이들 착물형성 과정에서의 엔탈피 및 엔트로피 변화, ${\Delta}$H 및 ${\Delta}$S는 10~40$^{\circ}C$ 온도 범위내에서 van't Hoff plot으로부터 구했으며, 이들의 값들은 각각, -2.71∼-3.79 kcal/mol과 -16.52∼-20.57 eu 범위내에 있었다.

• Bulletin of the Korean Chemical Society
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• 제32권3호
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• pp.921-926
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• 2011

This study investigates a root cause of the improved rate performance of $LiFePO_4$ after metal doping to Fesites. This is because the metal doped $LiFePO_4$/C maintains its initial capacity at higher C-rates than undoped one. Using $LiFePO_4$/C and doped $LiFe_{0.97}M_{0.03}PO_4$/C (M=$Al^{3+}$, $Cr^{3+}$, $Zr^{4+}$), which are synthesized by a mechanochemical process followed by one-step heat treatment, the Li content before and after chemical delithiation in the $LiFePO_4$/C and the binding energy are compared using atomic absorption spectroscopy (AAS) and X-ray photoelectron spectroscopy (XPS). The results from AAS and XPS indicate that the low Li content of the metal doped $LiFePO_4$/C after chemical delithiation is attributed to the low binding energy induced by weak Li-O interactions. The improved capacity retention of the doped $LiFePO_4$/C at high discharge rates is, therefore, achieved by relatively low binding energy between Li and O ions, which leads to fast Li diffusivity.

• Bulletin of the Korean Chemical Society
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• 제31권2호
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• pp.453-456
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• 2010

The structural and energetic preferences of thiacalix[4]biscrown-5 with and without alkali metal ions ($Na^+$, $K^+$, $Rb^+$, and $Cs^+$) have been theoretically investigated for the first time using molecular dynamic (MD) simulations and density functional theory (MPWB1K/6-31G(d)//B3LYP/6-31G(d)) methods. The formation of the metal ion complex by the host is mainly driven by the electrostatic attraction between crown-5 oxygens and a cation together with the minor contribution of the cation-$\pi$ interaction between two facing phenyl rings around the cation. The computed binding energies and the atomic charge distribution analysis for the metal binding complexes indicate the selectivity toward a potassium ion. The theoretical results herein explain the experimentally observed extractability order by this host towards various alkali metal ions. The physical nature and the driving forces for cation recognition by this host are discussed in detail.

• Toxicological Research
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• 제23권1호
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• pp.1-9
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• 2007

Transporters are membrane proteins that mediate the transfer of substrate across the cellular membrane. In this overview, the characteristics and the toxicological relevance were discussed for various types of transporters. For drug transporters, the overview focused on ATP-binding cassette transporters and solute carrier family 21A/22A member transporters. Except for OCTN transporters and OATP transporters, drug transporters tend to have broad substrate specificity, suggesting drug-drug interaction at the level of transport processes (e.g., interaction between methotrexate and non-steroidal anti-inflammatory agents) is likely. For metal transporters, transporters for zinc, copper and multiple metals were discussed in this overview. These metal transporters have comparatively narrow substrate specificity, except for multiple metal transporters, suggesting that inter-substrate interaction at the level of transport is less likely. In contrast, the expressions of the transporters are often regulated by their substrates, suggesting cellular adaptation mechanism exists for these transporters. The drug-drug interactions in drug transporters and the cellular adaptation mechanisms for metal transporters are likely to lead to alterations in pharmacokinetics and cellular metal homeostasis, which may be linked to the development of toxicity. Therefore, the transporter-mediated alterations may have toxicological relevance.

• Bulletin of the Korean Chemical Society
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• 제1권3호
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• pp.105-109
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• 1980

A general spectroscopic method is described for studies on the complex formation between metal ions and ligands, and is applied to $Cu^{2+}$ and $Ca^{2+}$binding to glycosaminoglycans. The order of binding constants for both ions is heparin >dermatan sulfate >chondroitin sulfate. The electrostatic forces are shown to be the predominant factor in the interaction. The 2- to 3-fold higher affinity for $Cu^{2+}$ than for $Ca^{2+}$ is obtained for heparin and dermatan sulfate, but little difference for chondroitin sulfate. These results are explained as chelation of both carboxyl and sulfate groups to $Cu^{2+}$ in former cases. The difference of binding constants among glycosaminoglycans is related to proposed various biological functions of the biopolymers.