Home > Publications database > The two distinctive metal ion binding domains of the wheat metallothionein Ec-1 > print

001     89739
005     20250718144922.0
024 7 _ |2 pmid
|a pmid:19111340
024 7 _ |2 doi
|a 10.1016/j.jinorgbio.2008.11.008
024 7 _ |2 ISSN
|a 0162-0134
024 7 _ |2 ISSN
|a 1873-3344
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|a WOS:000263693900005
024 7 _ |a openalex:W1965073499
|2 openalex
037 _ _ |a PHPPUBDB-15356
041 _ _ |a English
082 _ _ |a 540
100 1 _ |0 P:(DE-HGF)0
|a Peroza, E.
|b 0
|e Corresponding author
110 1 _ |a DESY
|b European Molecular Biology Laboratory
245 _ _ |a The two distinctive metal ion binding domains of the wheat metallothionein Ec-1
260 _ _ |a New York, NY [u.a.]
|b Elsevier
|c 2009
300 _ _ |a 342-353
336 7 _ |2 DRIVER
|a article
336 7 _ |2 DataCite
|a Output Types/Journal article
336 7 _ |0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
|a Journal Article
|b journal
|m journal
|s 1552333867_14794
336 7 _ |2 BibTeX
|a ARTICLE
336 7 _ |2 ORCID
|a JOURNAL_ARTICLE
336 7 _ |0 0
|2 EndNote
|a Journal Article
440 _ 0 |0 PERI:(DE-600)1491314-8
|a J. Inorg. Biochem.
|v 103
|x 0162-0134
|y 3
500 _ _ |3 Converted on 2013-05-30 13:45
|a (c) Elsevier B.V.; Post referee fulltext in progress 2; Embargo 12 months from publication
500 _ _ |3 Converted on 2013-06-21 19:20
520 _ _ |a Metallothioneins are small cysteine-rich proteins believed to play a role, among others, in the homeostasis of essential metal ions such as Zn(II) and Cu(I). Recently, we could show that wheat E(c)-1 is coordinating its six Zn(II) ions in form of metal-thiolate clusters analogously to the vertebrate metallothioneins. Specifically, two Zn(II) ions are bound in the N-terminal and four in the C-terminal domain. In the following, we will present evidence for the relative independence of the two domains from each other with respect to their metal ion binding abilities, and uncover three intriguing peculiarities of the protein. Firstly, one Zn(II) ion of the N-terminal domain is relative resistant to complete replacement with Cd(II) indicating the presence of a Zn(II)-binding site with increased stability. Secondly, the C-terminal domain is able to coordinate an additional fifth metal ion, though with reduced affinity, which went undetected so far. Finally, reconstitution of apoE(c)-1 with an excess of Zn(II) shows a certain amount of sub-stoichiometrically metal-loaded species. The possible relevance of these finding for the proposed biological functions of wheat E(c)-1 will be discussed. In addition, extended X-ray absorption fine structure (EXAFS) measurements on both, the full-length and the truncated protein, provide final evidence for His participation in metal ion binding.
536 _ _ |0 G:(DE-H253)POF1-DORIS-PETRA-20130405
|f POF I
|x 0
|c POF1-DORIS-PETRA-20130405
|a Facility (machine) DORIS/PETRA (POF1-DORIS-PETRA-20130405)
588 _ _ |a Dataset connected to Pubmed
650 _ 7 |0 0
|2 NLM Chemicals
|a Apoproteins
650 _ 7 |0 7440-43-9
|2 NLM Chemicals
|a Cadmium
650 _ 7 |0 7440-66-6
|2 NLM Chemicals
|a Zinc
650 _ 7 |0 9038-94-2
|2 NLM Chemicals
|a Metallothionein
650 _ 2 |2 MeSH
|a Apoproteins: metabolism
650 _ 2 |2 MeSH
|a Binding Sites
650 _ 2 |2 MeSH
|a Cadmium: metabolism
650 _ 2 |2 MeSH
|a Metallothionein: chemistry
650 _ 2 |2 MeSH
|a Metallothionein: genetics
650 _ 2 |2 MeSH
|a Metallothionein: metabolism
650 _ 2 |2 MeSH
|a Nuclear Magnetic Resonance, Biomolecular
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary: genetics
650 _ 2 |2 MeSH
|a Triticum: metabolism
650 _ 2 |2 MeSH
|a Zinc: metabolism
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|5 EXP:(DE-H253)DORISIII(machine)-20150101
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|e Facility (machine) DORIS III
|x 0
700 1 _ |a Kaabi, A.
|b 1
700 1 _ |a Meyer-Klaucke, W.
|b 2
700 1 _ |a Wellenreuther, G.
|b 3
700 1 _ |a Freisinger, E.
|b 4
773 _ _ |0 PERI:(DE-600)1491314-8
|a 10.1016/j.jinorgbio.2008.11.008
|g Vol. 103, p. 342-353
|p 342-353
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|t Journal of inorganic biochemistry
|v 103
|x 0162-0134
|y 2009
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