• 제목/요약/키워드: Zn-binding Ligands

검색결과 19건 처리시간 0.021초

Isolation and Transcriptional Expression of CuZn Superoxide Dismutase from Codonopsis lanceolata

  • Lee, Kang;In, Jun-Gyo;Yu, Chang-Yeon;Yun, Song-Joong;Min, Byung-Hoon;Rho, Yeong-Deok;Kim, Moo-Sung;Yang, Deok-Chun
    • Plant Resources
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    • 제7권3호
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    • pp.163-169
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    • 2004
  • To investigate the defense mechanism against the abiotic stress, a cDNA clone encoding a CuZn superoxide dismutase (CuZnSOD) protein was isolated from a cDNA library prepared from tabroot mRNAs of Codonopsis lanceolata. The eDNA, designated ClSODCc, is 799 nucleotides long and has an open reading frame of 459 bp with a deduced amino acid sequence of 152 residues. The deduced amino acid sequence of ClSODCc matched to the previously reported CuZnSODs. Consensus amino acid residues (His-45, -47, -62, -70, -79, -119 and Asp-82) were involved in Cu-, Cu/Zn-, and Zn- binding ligands. The deduced amino acid sequence of ClSODCc showed high homologies (82%-86%) regardless of species. Expression of ClSODCc by oxidative stress was increased up to 1 h after treatment and declined gradually. Much earlier and stronger expression of ClSODCc was observed in the cold stress treatment.

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Molecular Characterization and Expression of CuZn-superoxide Dismutase (PSOD1) from Populus alba${\times}$Populus glandulosa

  • Lee Jun-Won;In Jun-Gyo;Lee Bum-Soo;Choi Yong-Eui;Kim Jin-Ju;Yang Deok-Chun
    • Plant Resources
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    • 제8권1호
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    • pp.52-59
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    • 2005
  • A cDNA, PSOD1, encoding cytosolic copper/zinc superoxide dismutase (CuZn-SOD) was cloned and characterized from a full length cDNA library prepared from Populus alba${\times}$Populus glandulosa cultured in vitro. A PSOD1, is 725 nucleotides long and has an open reading frame of 459 bp with 152 amino acid residues (pI 5.43). The deduced amino acid sequence of PSOD1 perfect matched to the previously reported CuZn-SOD (CAC33845.1). Consensus amino acid residues (His-45, -47, -62, -70, -79, -119) were involved in Cu-, Cu/Zn-, and Zn- binding ligands. The deduced amino acid sequence of PSOD1 exhibited the high level of similarity from 100 to $85\%$ among previously registered SOD genes. The expression of PSOD1 in poplar increased at the 1 mM $H_{2}O_2$ and drought stress during 30 min and 60 min, but the ozone treated poplar increased at 30 min in the early time and then decreased at 60 min.

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Synthesis and Cations Binding Properties of a New C,N-bipyrazolic Ligand

  • Attayibat, Ahmed;Radi, Smaail;Ramdani, Abdelkrim;Lekchiri, Yahya;Hacht, Brahim;Bacquet, Maryse;Willai, Stephanie;Morcellet, Michel
    • Bulletin of the Korean Chemical Society
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    • 제27권10호
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    • pp.1648-1650
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    • 2006
  • The synthesis of a new C,N-bipyrazolic ligand with a functionalized donor-group is reported. The binding properties of the ligand and two other ligand of similar structures towards heavy metal ions ($Hg^{2+}$, $Cd^{2+}$, $Pb^{2+}$, $Zn^{2+}$, $Cu^{2+}$) and alkaline metal ions ($K^+$, $Na^{+}$, $Li^+$) were studied by a liquid-liquid extraction process and the extracted cation percentage was determined by atomic absorption measurements. The selectivity of the ligand to Hg(II) has been mentioned in the abstract.

Cloning and Characterization of the Cu,Zn Superoxide Dismutase (SOD1) cDNA from the Spider, Araneus ventricosus

  • Choi Young Soo;Choo Young Moo;Li Jianhong;Sohn Hung Dae;Jin Byung Rae
    • International Journal of Industrial Entomology and Biomaterials
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    • 제10권1호
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    • pp.73-77
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    • 2005
  • A Cu,Zn superoxide dismutase (SOD1) cDNA was cloned from the spider, Araneus ventricosus. The A. ventricosus SOD1 (AvSOD1) cDNA contains an open reading frame of 495 bp encoding 165 amino acid polypeptide with a predicted molecular mass of 17,114 Da and pI of 6.55, and possesses the typical metal binding ligands of six histidines and one aspartic acid common to SOD1s. The deduced amino acid sequence of the AvSOD1 cDNA showed $51\%$ identity to Ceratitis capitata SOD1, and $50\%$ to SOD1 sequences of both Drosophila melanogaster and Chymomyza amoena. Northern blot analysis revealed the presence of AvSOD1 transcripts in all tissues examined.

Isolation of Microcystin-LR and Its Potential Function of Ionophore

  • Kim, Gilhoon;Han, Seungwon;Won, Hoshik
    • 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.

Structure function relationships amongst the purple acid phosphatase family of binuclear metal-containing enzymes

  • Hamilton, Susan
    • 한국생물정보학회:학술대회논문집
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    • 한국생물정보시스템생물학회 2003년도 제2차 연례학술대회 발표논문집
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    • pp.5-5
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    • 2003
  • The purple acid phosphatases comprise a family of binuclear metal-containing enzymes. The metal centre contains one ferric ion and one divalent metal ion. Spectroscopic studies of the monomeric, ${\sim}$36 kDa mammalian purple acid phosphatases reveal the presence of an Fe(III)Fe(II) centre in which the metals are weakly antiferromagnetically coupled, whereas the dimeric, ${\sim}$110 000 kDa plant enzymes contain either Fe(III)Zn(II) or Fe(III)Mn(II). The three dimensional structures of the red kidney bean and pig enzymes show very similar arrangements of the metal ligands but some significant differences beyond the immediate vicinity of the metals. In addition to the catalytic domain, the plant enzyme contains a second domain of unknown function. A search of sequence databases was undertaken using a sequence pattern which includes the conserved metal-binding residues in the plant and animal enzymes. The search revealed the presence in plants of a 'mammalian-type' low molecular weight purple acid phosphatase, a high molecular weight form in some fungi, and a homologue in some bacteria. The catalytic mechanism of the enzyme has been investigated with a view to understanding the marked difference in specificity between the Fe-Mn sweet potato enzyme, which exhibits highly efficient catalysis towards both activated and unactivated phosphate esters, and other PAPs, which hydrolyse only activated esters. Comparison of the active site structures of the enzymes reveal some interesting differences between them which may account for the difference. The implications fur understanding the physiological functions of the enzymes will be discussed.

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Characterization of Copper/Zinc-Superoxide Dismutase (Cu/Zn-SOD) Gene from an Endangered Freshwater Fish Species Hemibarbus mylodon (Teleostei; Cypriniformes)

  • Lee, Sang-Yoon;Kim, Keun-Yong;Bang, In-Chul;Nam, Yoon-Kwon
    • Fisheries and Aquatic Sciences
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    • 제14권1호
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    • pp.43-54
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    • 2011
  • Gene structure of copper/zinc-superoxide dismutase (Cu/Zn-SOD; sod1) was characterized in Hemibarbus mylodon (Teleostei; Cypriniformes), an endangered freshwater fish species in Korean peninsula. Full-length cDNA of H. mylodon SOD1 consisted of a 796-bp open reading frame sequence encoding 154 amino acids, and the deduced polypeptide sequence shared high sequence homology with other orthologs, particularly with regard to metal-coordinating ligands. Genomic structure of the H. mylodon sod1 gene (hmsod1; 1,911 bp from the ATG start codon to the stop codon) was typical quinquepartite (i.e., five exons interrupted by four introns); the lengths of the exons were similar among species belonging to various taxonomic positions. The molecular phylogeny inferred from sod1 genes in the teleost lineage was in accordance with the conventional taxonomic assumptions. 5'-flanking upstream region of hmsod1, obtained using the genome walking method, contained typical TATA and CAAT boxes. It also showed various transcription factor binding motifs that may be potentially involved in stress/immune response (e.g., sites for activating proteins or nuclear factor kappa B) or metabolism of xenobiotic compounds (e.g., xenobiotic response element; XRE). The hmsod1 transcripts were ubiquitously detected among tissues, with the liver and spleen showing the highest and lowest expression, respectively. An experimental challenge with Edwardsiella tarda revealed significant upregulation of the hmsod1 in kidney (4.3-fold) and spleen (3.1-fold), based on a real-time RT-PCR assay. Information on the molecular characteristics of this key antioxidant enzyme gene could be a useful basis for a biomarker-based assay to understand cellular stresses in this endangered fish species.

Highly CO2-soluble 5-Amido-8-hydroxyquinoline Chelating Agents for Extraction of Metals in Sc-CO2

  • Chang, Fei;Park, Seo-Hun;Kim, Hakwon
    • Bulletin of the Korean Chemical Society
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    • 제29권7호
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    • pp.1327-1331
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    • 2008
  • Novel $CO_2$-soluble 8-hydroxyquinoline (8-HQ) chelating agents were synthesized and evaluated for solubility and metal ion extraction ability in supercritical $CO_2\;(Sc-CO_2)$. Among them, secondary amide-containing 8- HQ derivatives cannot be dispersed well into Sc-$CO_2$, but tertiary amide-containing derivatives can dissolve completely in Sc-$CO_2$ even at low CO2 pressures, perhaps owing to the predominant intermolecular interaction between the chelating agent and the $CO_2$ molecule. Based on 8-HQ chelating agent solubility data, we investigated the extraction of metal ions ($Co^{2+}$, $Cu^{2+}$, $Sr^{2+}$, $Cd^{2+}$, and $Zn^{2+}$) using two highly $CO_2$-soluble 8-HQ derivatives (4d, 4e) in Sc-$CO_2$. The extraction efficiency of tertiary amide-containing 8-HQ ligands, both fluorinated and non-fluorinated forms, was dramatically increased in the presence of diethyl amine (organic base). We suggest that diethyl amine could play an important synergistic role in the stronger metal binding ability of 8-HQ through an in situ deprotonation reaction in Sc-$CO_2$ medium.

총알고둥에서 카드뮴과 아연의 축적과 제거 (Accumulation and Elimination of Cadmium and Zinc in Littorina brevicula)

  • 한수정;이인숙
    • The Korean Journal of Ecology
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    • 제24권1호
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    • pp.35-43
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    • 2001
  • 카드뮴과 아연에 각각 그리고 동시에 노출한 총알고둥(Littorina brevicula)에서 중금속의 생체내 축적, 제거 및 세포내 분포 양상을 조사하였다. 총알고둥을 카드뮴 400 $\mu\textrm{g}$/L 또는 아연 3000 $\mu\textrm{g}$/L에 각각 90일간 노출하였을 경우, 각 중금속의 축적량은 노출기간에 따라 증가하였으며, 70일 이후에는 더 이상 축적량이 증가하지 않았다. 카드뮴과 아연을 동시에 노출하였을 경우에는 각각의 중금속에 노출하였을 경우에 비해 아연의 축적량은 증가하였으나, 카드뮴의 축적량은 감소하였다. 노출실험에 이어 수행한 42일간의 청장실험 결과, 카드뮴은 체외로 제거되지 않았으나, 아연은 제거되었다. 특히 카드뮴과 아연에 동시 노출한 총알고둥의 경우에 아연은 더 신속히 제거되었다. 총알고둥을 카드뮴과 아연에 각각 70일 동안 노출한 후, 체내로 흡수된 카드뮴의 약 60%가 soluble fraction에 분포하고 있었으며, 아연의 75%는 insoluble fraction에 분포하고 있었다. 이러한 경향은 카드뮴과 아연의 동시 노출시에도 유사하게 나타났다. 카드뮴과 아연은 soluble part내의 리간드(ligand) 와의 결합 양상에서도 차이를 나타냈는데, 카드뮴은 90% 이상이 약 6.5 kDa크기의 MBP-1(Metal-Binding Protein-1)과 결합하고 있었으나, 아연은 HMW(High molecular weight fraction, >60 kDa), MBP-1, MBP-2, LMW(Low molecular weight fraction <1 kDa)에 고루 분포하는 것으로 나타났다.

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