Cadmium inhibitory action leads to changes in structure of ferredoxin:NADP+ oxidoreductase

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• 作者：Joanna Grzyb (12) jgrzyb@ifpan.edu.pl
  Mariusz Gago? (34) mariusz.gagos@up.lublin.pl
  Beata My?liwa-Kurdziel (1) b.mysliwa-kurdziel@uj.edu.pl
  Monika Bojko (1) monika.bojko@uj.edu.pl
  Wies?aw I. Gruszecki (5) wieslaw.gruszecki@umcs.pl
  Andrzej Waloszek (1) andrzej.waloszek@uj.edu.pl
  Kazimierz Strza?ka (1) strzalka@mol.uj.edu.pl
• 关键词：Ferredoxin ; NADP+ oxidoreductase – Cadmium – Heavy metals – Secondary structure – Tertiary structure
• 刊名：Journal of Biological Physics
• 出版年：2012
• 出版时间：June 2012
• 年：2012
• 卷：38
• 期：3
• 页码：415-428
• 全文大小：560.5 KB
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• 作者单位：1. Department of Plant Physiology and Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, ul. Gronostajowa 7, 30-387 Krakow, Poland2. Laboratory of Biological Physics, Institute of Physics, PAS, al. Lotników 32/46, 02-668 Warsaw, Poland3. Department of Biophysics, University of Life Sciences in Lublin, Akademicka 13, 20-950 Lublin, Poland4. Department of Cell Biology, Institute of Biology, Maria Curie-Sk?odowska University, 20-033 Lublin, Poland5. Department of Biophysics, Maria Sklodowska-Curie University, Lublin, Poland
• ISSN：1573-0689

文摘

This study deals with the influence of cadmium on the structure and function of ferredoxin:NADP+ oxidoreductase (FNR), one of the key photosynthetic enzymes. We describe changes in the secondary and tertiary structure of the enzyme upon the action of metal ions using circular dichroism measurements, Fourier transform infrared spectroscopy and fluorometry, both steady-state and time resolved. The decrease in FNR activity corresponds to a gentle unfolding of the protein, caused mostly by a nonspecific binding of metal ions to multiple sites all over the enzyme molecule. The final inhibition event is most probably related to a bond created between cadmium and cysteine in close proximity to the FNR active center. As a result, the flavin cofactor is released. The cadmium effect is compared to changes related to ionic strength and other ions known to interact with cysteine. The complete molecular mechanism of FNR inhibition by heavy metals is discussed.