Synthesis of Iron Oxide Nanoparticles in Listeria innocua Dps (DNA-Binding Protein from Starved Cells): A Study with the Wild-Type Protein and a Catalytic Centre Mutant (Articolo in rivista)

Type
Label
  • Synthesis of Iron Oxide Nanoparticles in Listeria innocua Dps (DNA-Binding Protein from Starved Cells): A Study with the Wild-Type Protein and a Catalytic Centre Mutant (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/chem.200901138 (literal)
Alternative label
  • Ceci P, Chiancone E, Kasyutich O, Bellapadrona G, Castelli L, Fittipaldi M, Gatteschi D, Innocenti C, Sangregorio C. (2010)
    Synthesis of Iron Oxide Nanoparticles in Listeria innocua Dps (DNA-Binding Protein from Starved Cells): A Study with the Wild-Type Protein and a Catalytic Centre Mutant
    in Chemistry (Weinh., Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ceci P, Chiancone E, Kasyutich O, Bellapadrona G, Castelli L, Fittipaldi M, Gatteschi D, Innocenti C, Sangregorio C. (literal)
Pagina inizio
  • 709 (literal)
Pagina fine
  • 717 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 16 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1. Univ Florence, La MM Dept Chem, I-50019 Sesto Fiorentino, FI, Italy 2. Univ Rome, CNR, Inst Mol Biol & Pathol, Dept Biochem Sci A Rossi Fanelli Sapienza, I-00185 Rome, Italy 3. Univ Bristol, Dept Phys, H Will Phys Lab, Bristol BS8 1TL, Avon, England (literal)
Titolo
  • Synthesis of Iron Oxide Nanoparticles in Listeria innocua Dps (DNA-Binding Protein from Starved Cells): A Study with the Wild-Type Protein and a Catalytic Centre Mutant (literal)
Abstract
  • A comparative analysis of the magnetic properties of iron oxide nanoparticles grown in the cavity of the DNA-binding protein from starved cells of the bacterium Listeria innocua, LiDps, and of its triple-mutant lacking the catalytic ferroxidase centre, LiDps-tm, is presented. TEM images and static and dynamic magnetic and electron magnetic resonance (EMR) measurements reveal that, under the applied preparation conditions, namely alkaline pH, high temperature (65 degrees C), exclusion of oxygen, and the presence of hydrogen peroxide, maghemite and/or magnetite nanoparticles with an average diameter of about 3 nm are mineralised inside the cavities of both LiDps and LiDps-tm. The magnetic nanoparticles (MNPs) thus formed show similar magnetic properties, with superparamagnetic behaviour above 4.5 K and a large magnetic anisotropy. Interestingly, in the EMR spectra ail absorption at half-field is observed, which call be considered as a manifestation of the quantum behaviour of the MNPs. These results indicate that Dps proteins call be advantageously used for the production of nanomagnets at the interface between molecular Clusters and traditional MNPs and that the presence of the ferroxidase centre, though increasing the efficiency of nanoparticle formation, does not affect the nature and fine structure of the MNPs. Importantly, the self-organisation of MNP-containing Dps on HRTEM grids suggests that Dps-enclosed MNPs can be deposited oil surfaces in ail ordered fashion. (literal)
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