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.
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 an absorption at half-field is observed, which can be considered as a manifestation of the quantum behaviour of the MNPs. These results indicate that Dps proteins can 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 on surfaces in an ordered fashion.
C.N.R. Institute of Molecular Biology and Pathology, Department of Biochemical Sciences A. Rossi-Fanelli, Sapienza, University of Rome, 00185 Rome, Italy.
Pierpaolo
P
Ceci
Emilia
E
Chiancone
Oksana
O
Kasyutich
Giuliano
G
Bellapadrona
Lisa
L
Castelli
Maria
M
Fittipaldi
Dante
D
Gatteschi
Claudia
C
Innocenti
Claudio
C
Sangregorio
D001426:Bacterial Proteins / Q000378:metabolism* / Q000648:ultrastructure; D002384:Catalysis; D002570:Ceruloplasmin / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism* / Q000648:ultrastructure; D005290:Ferric Compounds / Q000138:chemical synthesis* / Q000378:metabolism; D008087:Listeria / Q000235:genetics / Q000378:metabolism*; D053758:Nanoparticles
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C083911:DPS protein, Bacteria; D005290:Ferric Compounds; C000499:ferric oxide; D002570:Ceruloplasmin