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@ARTICLE{Peroza:89739,
      author       = {Peroza, E. and Kaabi, A. and Meyer-Klaucke, W. and
                      Wellenreuther, G. and Freisinger, E. and DESY},
      title        = {{T}he two distinctive metal ion binding domains of the
                      wheat metallothionein {E}c-1},
      journal      = {Journal of inorganic biochemistry},
      volume       = {103},
      issn         = {0162-0134},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PHPPUBDB-15356},
      pages        = {342-353},
      year         = {2009},
      note         = {(c) Elsevier B.V.; Post referee fulltext in progress 2;
                      Embargo 12 months from publication},
      abstract     = {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.},
      keywords     = {Apoproteins: metabolism / Binding Sites / Cadmium:
                      metabolism / Metallothionein: chemistry / Metallothionein:
                      genetics / Metallothionein: metabolism / Nuclear Magnetic
                      Resonance, Biomolecular / Protein Conformation / Protein
                      Structure, Tertiary: genetics / Triticum: metabolism / Zinc:
                      metabolism / Apoproteins (NLM Chemicals) / Cadmium (NLM
                      Chemicals) / Zinc (NLM Chemicals) / Metallothionein (NLM
                      Chemicals)},
      cin          = {HASYLAB(-2012) / EMBL(-2012)},
      ddc          = {540},
      cid          = {$I:(DE-H253)HASYLAB_-2012_-20130307$ /
                      $I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {Facility (machine) DORIS/PETRA (POF1-DORIS-PETRA-20130405)},
      pid          = {G:(DE-H253)POF1-DORIS-PETRA-20130405},
      experiment   = {EXP:(DE-H253)DORISIII(machine)-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19111340},
      UT           = {WOS:000263693900005},
      doi          = {10.1016/j.jinorgbio.2008.11.008},
      url          = {https://bib-pubdb1.desy.de/record/89739},
}