Magnetic properties and structural characterization of iron oxide nanoparticles formed by Streptococcus suis Dpr and four mutants
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| Titel: | Magnetic properties and structural characterization of iron oxide nanoparticles formed by Streptococcus suis Dpr and four mutants |
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| Autoren: | Haikarainen, T., Paturi, P., Linden, J., Haataja, S., Meyer-Klaucke, W., Finne, J., Papageorgiou, A. C. |
| Quelle: | Journal of biological inorganic chemistry 16, 799-807 (2011). doi:10.1007/s00775-011-0781-z |
| Verlagsinformationen: | Springer Science and Business Media LLC, 2011. |
| Publikationsjahr: | 2011 |
| Schlagwörter: | 0301 basic medicine, Ferric Compounds: metabolism, Streptococcus suis: genetics, Streptococcus suis, Crystallography, X-Ray, Protein Engineering, 01 natural sciences, Ferric Compounds, Nanoparticles: chemistry, Magnetics, Spectroscopy, Mossbauer, 03 medical and health sciences, Bacterial Proteins, Bacterial Proteins: chemistry, Point Mutation, Streptococcus suis: metabolism, 0303 health sciences, ta1182, Ceruloplasmin, Streptococcus suis: chemistry, Bacterial Proteins: metabolism, 0104 chemical sciences, Ferric Compounds: chemistry, ferric oxide, Ferritins, Ferritins: metabolism, Nanoparticles, Ceruloplasmin: metabolism, Bacterial Proteins: genetics |
| Beschreibung: | 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. |
| Publikationsart: | Article |
| Sprache: | English |
| ISSN: | 1432-1327 0949-8257 |
| DOI: | 10.1007/s00775-011-0781-z |
| Zugangs-URL: | http://bib-pubdb1.desy.de/record/95049 https://pubmed.ncbi.nlm.nih.gov/21487937 http://juuli.fi/Record/0050626811 https://link.springer.com/article/10.1007/s00775-011-0781-z https://core.ac.uk/display/20513456 http://europepmc.org/abstract/MED/21487937 https://link.springer.com/content/pdf/10.1007%2Fs00775-011-0781-z.pdf https://research.abo.fi/en/publications/magnetic-properties-and-structural-characterization-of-iron-oxide https://bib-pubdb1.desy.de/record/95049 |
| Rights: | Springer TDM |
| Dokumentencode: | edsair.doi.dedup.....2a6e49e18419ff5bb56ad74aa3bb6d6d |
| Datenbank: | OpenAIRE |
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Nájsť tento článok vo Web of Science | 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. |
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| ISSN: | 14321327 09498257 |
| DOI: | 10.1007/s00775-011-0781-z |