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Please use this identifier to cite or link to this item: http://hdl.handle.net/10119/8550

Title: Chelation of cadmium ions by phytochelatin synthas  : role of the cystein-rich C-terminal
Authors: VESTERGAARD, Mun'delanji
MATSUMOTO, Sachiko
NISHIKORI, Shingo
SHIRAKI, Kentaro
HIRATA, Kazumasa
TAKAGI, Masahiro
Issue Date: 2008-02
Publisher: 日本分析化学会
Magazine name: Analytical Sciences
Volume: 24
Number: 2
Start page: 277
End page: 281
DOI: 10.2116/analsci.24.277
Abstract: 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.
Rights: Copyright (C) 2008 日本分析化学会. Mun'delanji VESTERGAARD, Sachiko MATSUMOTO, Shingo NISHIKORI, Kentaro SHIRAKI, Kazumasa HIRATA, Masahiro TAKAGI, Analytical Sciences, 24(2), 2008, 277-281. http://dx.doi.org/10.2116/analsci.24.277
URI: http://hdl.handle.net/10119/8550
Material Type: publisher
Appears in Collections:c10-1. 雑誌掲載論文 (Journal Articles)

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