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001     95049
005     20250803044642.0
024 7 _ |a pmid:21487937
|2 pmid
024 7 _ |a 10.1007/s00775-011-0781-z
|2 doi
024 7 _ |a 1432-1327
|2 ISSN
024 7 _ |a 0949-8257
|2 ISSN
024 7 _ |a WOS:000290773500012
|2 WOS
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024 7 _ |a altmetric:143072997
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037 _ _ |a PHPPUBDB-19320
041 _ _ |a eng
082 _ _ |a 540
100 1 _ |a Haikarainen, T.
110 1 _ |a DESY
|b European Molecular Biology Laboratory
245 _ _ |a Magnetic properties and structural characterization of iron oxide nanoparticles formed by Streptococcus suis Dpr and four mutants
260 _ _ |a Berlin
|b Springer
|c 2011
300 _ _ |a 799-807
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a article
|2 DRIVER
336 7 _ |a Journal Article
|b journal
|m journal
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a ARTICLE
|2 BibTeX
440 _ 0 |0 PERI:(DE-600)1464026-0
|a J. Biol. Inorg. Chem.
|v 16
|x 0949-8257
500 _ _ |3 Converted on 2013-05-30 15:11
500 _ _ |3 Converted on 2013-06-21 19:21
520 _ _ |a 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.
536 _ _ |0 G:(DE-H253)POF2-K1.2-20130405
|f POF II
|x 0
|c POF2-54G13
|a DORIS Beamline K1.2 (POF2-54G13)
588 _ _ |a Dataset connected to Pubmed
650 _ 7 |0 0
|2 NLM Chemicals
|a Bacterial Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Ferric Compounds
650 _ 7 |0 1309-37-1
|2 NLM Chemicals
|a ferric oxide
650 _ 7 |0 9007-73-2
|2 NLM Chemicals
|a Ferritins
650 _ 7 |0 EC 1.16.3.1
|2 NLM Chemicals
|a Ceruloplasmin
650 _ 2 |2 MeSH
|a Bacterial Proteins: chemistry
650 _ 2 |2 MeSH
|a Bacterial Proteins: genetics
650 _ 2 |2 MeSH
|a Bacterial Proteins: metabolism
650 _ 2 |2 MeSH
|a Ceruloplasmin: metabolism
650 _ 2 |2 MeSH
|a Crystallography, X-Ray
650 _ 2 |2 MeSH
|a Ferric Compounds: chemistry
650 _ 2 |2 MeSH
|a Ferric Compounds: metabolism
650 _ 2 |2 MeSH
|a Ferritins: metabolism
650 _ 2 |2 MeSH
|a Magnetics
650 _ 2 |2 MeSH
|a Nanoparticles: chemistry
650 _ 2 |2 MeSH
|a Point Mutation
650 _ 2 |2 MeSH
|a Protein Engineering
650 _ 2 |2 MeSH
|a Spectroscopy, Mossbauer
650 _ 2 |2 MeSH
|a Streptococcus suis: chemistry
650 _ 2 |2 MeSH
|a Streptococcus suis: genetics
650 _ 2 |2 MeSH
|a Streptococcus suis: metabolism
693 _ _ |a DORIS III
|f DORIS Beamline K1.2
|1 EXP:(DE-H253)DORISIII-20150101
|0 EXP:(DE-H253)D-K1.2-20150101
|6 EXP:(DE-H253)D-K1.2-20150101
|x 0
700 1 _ |a Paturi, P.
700 1 _ |a Linden, J.
700 1 _ |a Haataja, S.
700 1 _ |a Meyer-Klaucke, W.
700 1 _ |a Finne, J.
700 1 _ |a Papageorgiou, A. C.
773 _ _ |0 PERI:(DE-600)1464026-0
|a 10.1007/s00775-011-0781-z
|g Vol. 16, p. 799-807
|p 799-807
|q 16<799-807
|t Journal of biological inorganic chemistry
|v 16
|x 0949-8257
|y 2011
856 4 _ |u https://bib-pubdb1.desy.de/record/95049/files/jbic-1-revision-main-text.doc
|y OpenAccess
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|l Forschung mit Photonen, Neutronen, Ionen
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