% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Haikarainen:95049,
      author       = {Haikarainen, T. and Paturi, P. and Linden, J. and Haataja,
                      S. and Meyer-Klaucke, W. and Finne, J. and Papageorgiou, A.
                      C. and DESY},
      title        = {{M}agnetic properties and structural characterization of
                      iron oxide nanoparticles formed by {S}treptococcus suis
                      {D}pr and four mutants},
      journal      = {Journal of biological inorganic chemistry},
      volume       = {16},
      issn         = {0949-8257},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {PHPPUBDB-19320},
      pages        = {799-807},
      year         = {2011},
      abstract     = {Streptococcus suis Dpr belongs to the Dps family of
                      bacterial and archaeal proteins that oxidize Fe(2+) to
                      Fe(3+) to protect microorganisms from oxidative damage. The
                      oxidized iron is subsequently deposited as ferrihydrite
                      inside a protein cavity, resulting in the formation of an
                      iron core. The size and the magnetic properties of the iron
                      core have attracted considerable attention for
                      nanotechnological applications in recent years. Here, the
                      magnetic and structural properties of the iron core in
                      wild-type Dpr and four cavity mutants were studied. All
                      samples clearly demonstrated a superparamagnetic behavior in
                      superconducting quantum interference device magnetometry and
                      Mössbauer spectroscopy compatible with that of
                      superparamagnetic ferrihydrite nanoparticles. However, all
                      the mutants exhibited higher magnetic moments than the
                      wild-type protein. Furthermore, measurement of the iron
                      content with inductively coupled plasma mass spectrometry
                      revealed a smaller amount of iron in the iron cores of the
                      mutants, suggesting that the mutations affect nucleation and
                      iron deposition inside the cavity. The X-ray crystal
                      structures of the mutants revealed no changes compared with
                      the wild-type crystal structure; thus, the differences in
                      the magnetic moments could not be attributed to structural
                      changes in the protein. Extended X-ray absorption fine
                      structure measurements showed that the coordination geometry
                      of the iron cores of the mutants was similar to that of the
                      wild-type protein. Taken together, these results suggest
                      that mutation of the residues that surround the iron storage
                      cavity could be exploited to selectively modify the magnetic
                      properties of the iron core without affecting the structure
                      of the protein and the geometry of the iron core.},
      keywords     = {Bacterial Proteins: chemistry / Bacterial Proteins:
                      genetics / Bacterial Proteins: metabolism / Ceruloplasmin:
                      metabolism / Crystallography, X-Ray / Ferric Compounds:
                      chemistry / Ferric Compounds: metabolism / Ferritins:
                      metabolism / Magnetics / Nanoparticles: chemistry / Point
                      Mutation / Protein Engineering / Spectroscopy, Mossbauer /
                      Streptococcus suis: chemistry / Streptococcus suis: genetics
                      / Streptococcus suis: metabolism / Bacterial Proteins (NLM
                      Chemicals) / Ferric Compounds (NLM Chemicals) / ferric oxide
                      (NLM Chemicals) / Ferritins (NLM Chemicals) / Ceruloplasmin
                      (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {540},
      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:21487937},
      UT           = {WOS:000290773500012},
      doi          = {10.1007/s00775-011-0781-z},
      url          = {https://bib-pubdb1.desy.de/record/95049},
}