Chelation of Cadmium Ions by Phytochelatin Synthase : Role of the Cystein-rich C-Terminal

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The interactions between Cd^<2+> and the C-terminal region of phytochelatin (PC) synthase using recombinant wild-type and mutant PC synthase were studied. We show that site-directed mutagenesis of Cys residues at C^<358>C^<359>XXXC^<363>XXC^<366> motif decreases the number of Cd^<2+> and other heavy metal ions interacting with the enzyme, and that the motif binds the metals discriminatingly. The optimum binding ratio of PC synthase to Cd^<2+> was also determined. The findings indicate that Cys exists as a free SH residue and that it is involved in the regulation of PC enzyme activity by transferring the metals into closer proximity with the catalytic domain. These results are important in understanding heavy metal detoxification mechanisms in higher plants, a step towards phytoremediated-applications.

収録刊行物

  • Analytical sciences : the international journal of the Japan Society for Analytical Chemistry  

    Analytical sciences : the international journal of the Japan Society for Analytical Chemistry 24(2), 277-281, 2008-02-10 

    日本分析化学会

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各種コード

  • NII論文ID(NAID)
    10021098648
  • NII書誌ID(NCID)
    AA10500785
  • 本文言語コード
    ENG
  • 資料種別
    NOT
  • ISSN
    09106340
  • NDL 記事登録ID
    9362966
  • NDL 雑誌分類
    ZP4(科学技術--化学・化学工業--分析化学)
  • NDL 請求記号
    Z54-F482
  • データ提供元
    CJP書誌  NDL  IR 
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