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@ARTICLE{Haikarainen:97456,
      author       = {Haikarainen, T. and Papageorgiou, A. C. and Tsoub, C.-C.
                      and Wub, J.-J. and DESY},
      title        = {{S}tructural characterization and biological implications
                      of di-zinc binding in the ferroxidase center of
                      {S}treptococcus pyogenes {D}pr.},
      journal      = {Biochemical and biophysical research communications},
      volume       = {398},
      issn         = {0006-291X},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PHPPUBDB-20419},
      pages        = {361-365},
      year         = {2010},
      abstract     = {Dps proteins contain a ferroxidase site that binds and
                      oxidizes iron, thereby preventing hydroxyl radical formation
                      by Fenton reaction. Although the involvement of a di-iron
                      ferroxidase site has been suggested, X-ray crystal
                      structures of various Dps members have shown either one or
                      two iron cations with various occupancies despite the high
                      structural conservation of the site. Similarly, structural
                      studies with zinc, a redox-stable replacement for iron, have
                      shown the binding of either one or two zinc ions. Here, the
                      crystal structure of Streptococcus pyogenes Dpr in complex
                      with zinc reveals the binding of two zinc cations in the
                      ferroxidase center and an additional zinc-binding site at
                      the surface of the protein. The results suggest a structural
                      basis for the protection of Streptococcus pyogenes in zinc
                      stress conditions and provide a clear evidence for a di-zinc
                      and di-iron ferroxidase site in Streptococcus pyogenes Dpr
                      protein.},
      keywords     = {Bacterial Proteins: chemistry / Bacterial Proteins:
                      genetics / Binding Sites / Ceruloplasmin: chemistry /
                      Ceruloplasmin: genetics / Crystallography, X-Ray /
                      DNA-Binding Proteins: chemistry / DNA-Binding Proteins:
                      genetics / Protein Conformation / Streptococcus pyogenes:
                      enzymology / Zinc: chemistry / Bacterial Proteins (NLM
                      Chemicals) / DNA-Binding Proteins (NLM Chemicals) / Dpr
                      protein, Streptococcus (NLM Chemicals) / Zinc (NLM
                      Chemicals) / Ceruloplasmin (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline K1.2 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-K1.2-20130405},
      experiment   = {EXP:(DE-H253)D-K1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20599728},
      UT           = {WOS:000280867400005},
      doi          = {10.1016/j.bbrc.2010.06.071},
      url          = {https://bib-pubdb1.desy.de/record/97456},
}