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000095049 1001_ $$aHaikarainen, T.
000095049 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000095049 245__ $$aMagnetic properties and structural characterization of iron oxide nanoparticles formed by Streptococcus suis Dpr and four mutants
000095049 260__ $$aBerlin$$bSpringer$$c2011
000095049 300__ $$a799-807
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000095049 440_0 $$0PERI:(DE-600)1464026-0$$aJ. Biol. Inorg. Chem.$$v16$$x0949-8257
000095049 500__ $$3Converted on 2013-05-30 15:11
000095049 500__ $$3Converted on 2013-06-21 19:21
000095049 520__ $$aStreptococcus suis Dpr belongs to the Dps family of bacterial and archaeal proteins that oxidize Fe(2+) to Fe(3+) to protect microorganisms from oxidative damage. The oxidized iron is subsequently deposited as ferrihydrite inside a protein cavity, resulting in the formation of an iron core. The size and the magnetic properties of the iron core have attracted considerable attention for nanotechnological applications in recent years. Here, the magnetic and structural properties of the iron core in wild-type Dpr and four cavity mutants were studied. All samples clearly demonstrated a superparamagnetic behavior in superconducting quantum interference device magnetometry and Mössbauer spectroscopy compatible with that of superparamagnetic ferrihydrite nanoparticles. However, all the mutants exhibited higher magnetic moments than the wild-type protein. Furthermore, measurement of the iron content with inductively coupled plasma mass spectrometry revealed a smaller amount of iron in the iron cores of the mutants, suggesting that the mutations affect nucleation and iron deposition inside the cavity. The X-ray crystal structures of the mutants revealed no changes compared with the wild-type crystal structure; thus, the differences in the magnetic moments could not be attributed to structural changes in the protein. Extended X-ray absorption fine structure measurements showed that the coordination geometry of the iron cores of the mutants was similar to that of the wild-type protein. Taken together, these results suggest that mutation of the residues that surround the iron storage cavity could be exploited to selectively modify the magnetic properties of the iron core without affecting the structure of the protein and the geometry of the iron core.
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000095049 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000095049 650_7 $$00$$2NLM Chemicals$$aFerric Compounds
000095049 650_7 $$01309-37-1$$2NLM Chemicals$$aferric oxide
000095049 650_7 $$09007-73-2$$2NLM Chemicals$$aFerritins
000095049 650_7 $$0EC 1.16.3.1$$2NLM Chemicals$$aCeruloplasmin
000095049 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000095049 650_2 $$2MeSH$$aBacterial Proteins: genetics
000095049 650_2 $$2MeSH$$aBacterial Proteins: metabolism
000095049 650_2 $$2MeSH$$aCeruloplasmin: metabolism
000095049 650_2 $$2MeSH$$aCrystallography, X-Ray
000095049 650_2 $$2MeSH$$aFerric Compounds: chemistry
000095049 650_2 $$2MeSH$$aFerric Compounds: metabolism
000095049 650_2 $$2MeSH$$aFerritins: metabolism
000095049 650_2 $$2MeSH$$aMagnetics
000095049 650_2 $$2MeSH$$aNanoparticles: chemistry
000095049 650_2 $$2MeSH$$aPoint Mutation
000095049 650_2 $$2MeSH$$aProtein Engineering
000095049 650_2 $$2MeSH$$aSpectroscopy, Mossbauer
000095049 650_2 $$2MeSH$$aStreptococcus suis: chemistry
000095049 650_2 $$2MeSH$$aStreptococcus suis: genetics
000095049 650_2 $$2MeSH$$aStreptococcus suis: metabolism
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000095049 7001_ $$aPaturi, P.
000095049 7001_ $$aLinden, J.
000095049 7001_ $$aHaataja, S.
000095049 7001_ $$aMeyer-Klaucke, W.
000095049 7001_ $$aFinne, J.
000095049 7001_ $$aPapageorgiou, A. C.
000095049 773__ $$0PERI:(DE-600)1464026-0$$a10.1007/s00775-011-0781-z$$gVol. 16, p. 799-807$$p799-807$$q16<799-807$$tJournal of biological inorganic chemistry$$v16$$x0949-8257$$y2011
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