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000089739 1001_ $$0P:(DE-HGF)0$$aPeroza, E.$$b0$$eCorresponding author
000089739 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000089739 245__ $$aThe two distinctive metal ion binding domains of the wheat metallothionein Ec-1
000089739 260__ $$aNew York, NY [u.a.]$$bElsevier$$c2009
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000089739 440_0 $$0PERI:(DE-600)1491314-8$$aJ. Inorg. Biochem.$$v103$$x0162-0134$$y3
000089739 500__ $$3Converted on 2013-05-30 13:45$$a(c) Elsevier B.V.; Post referee fulltext in progress 2; Embargo 12 months from publication
000089739 500__ $$3Converted on 2013-06-21 19:20
000089739 520__ $$aMetallothioneins are small cysteine-rich proteins believed to play a role, among others, in the homeostasis of essential metal ions such as Zn(II) and Cu(I). Recently, we could show that wheat E(c)-1 is coordinating its six Zn(II) ions in form of metal-thiolate clusters analogously to the vertebrate metallothioneins. Specifically, two Zn(II) ions are bound in the N-terminal and four in the C-terminal domain. In the following, we will present evidence for the relative independence of the two domains from each other with respect to their metal ion binding abilities, and uncover three intriguing peculiarities of the protein. Firstly, one Zn(II) ion of the N-terminal domain is relative resistant to complete replacement with Cd(II) indicating the presence of a Zn(II)-binding site with increased stability. Secondly, the C-terminal domain is able to coordinate an additional fifth metal ion, though with reduced affinity, which went undetected so far. Finally, reconstitution of apoE(c)-1 with an excess of Zn(II) shows a certain amount of sub-stoichiometrically metal-loaded species. The possible relevance of these finding for the proposed biological functions of wheat E(c)-1 will be discussed. In addition, extended X-ray absorption fine structure (EXAFS) measurements on both, the full-length and the truncated protein, provide final evidence for His participation in metal ion binding.
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000089739 650_7 $$00$$2NLM Chemicals$$aApoproteins
000089739 650_7 $$07440-43-9$$2NLM Chemicals$$aCadmium
000089739 650_7 $$07440-66-6$$2NLM Chemicals$$aZinc
000089739 650_7 $$09038-94-2$$2NLM Chemicals$$aMetallothionein
000089739 650_2 $$2MeSH$$aApoproteins: metabolism
000089739 650_2 $$2MeSH$$aBinding Sites
000089739 650_2 $$2MeSH$$aCadmium: metabolism
000089739 650_2 $$2MeSH$$aMetallothionein: chemistry
000089739 650_2 $$2MeSH$$aMetallothionein: genetics
000089739 650_2 $$2MeSH$$aMetallothionein: metabolism
000089739 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000089739 650_2 $$2MeSH$$aProtein Conformation
000089739 650_2 $$2MeSH$$aProtein Structure, Tertiary: genetics
000089739 650_2 $$2MeSH$$aTriticum: metabolism
000089739 650_2 $$2MeSH$$aZinc: metabolism
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000089739 7001_ $$aKaabi, A.$$b1
000089739 7001_ $$aMeyer-Klaucke, W.$$b2
000089739 7001_ $$aWellenreuther, G.$$b3
000089739 7001_ $$aFreisinger, E.$$b4
000089739 773__ $$0PERI:(DE-600)1491314-8$$a10.1016/j.jinorgbio.2008.11.008$$gVol. 103, p. 342-353$$p342-353$$q103<342-353$$tJournal of inorganic biochemistry$$v103$$x0162-0134$$y2009
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