|
JAIST Repository >
School of Materials Science >
Articles >
Journal Articles >
Please use this identifier to cite or link to this item:
https://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: | https://hdl.handle.net/10119/8550 |
| Material Type: | publisher |
| Appears in Collections: | c10-1. 雑誌掲載論文 (Journal Articles)
|
Files in This Item:
| File |
Description |
Size | Format |
|---|
| 13541.pdf | | 121Kb | Adobe PDF | View/Open |
|
All items in DSpace are protected by copyright, with all rights reserved.
|
