Metal ion binding to apo, holo, and reconstituted horse spleen ferritin☆
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The application of ferritin in transporting and binding diverse metal ions
2024, Food ChemistryMagnetoferritin enhances T<inf>2</inf> contrast in magnetic resonance imaging of macrophages
2021, Materials Science and Engineering CCitation Excerpt :Reducing agents, such as ascorbic acid and cofactor NAD(P)H, interact with iron core and reduce Fe3+ back to soluble Fe2+ forms [22–24]. Moreover, ferritin core are found to bind non-standard metal ions and small molecules [25–29]. The ability to bind different paramagnetic metal ions makes it a good template for controlled synthesis of various metal nanoparticles.
Integrative proteomics and metabolomics profiling of the protective effects of Phascolosoma esculent ferritin on BMSCs in Cd(II) injury
2021, Ecotoxicology and Environmental SafetyDesigning Peptide Bunches on Nanocage for Bispecific or Superaffinity Targeting
2016, BiomacromoleculesFerritin family proteins and their use in bionanotechnology
2015, New BiotechnologyCitation Excerpt :To get around this limitation reconstitution and washing of the ferritin cage has been used to optimise the production of gold nanoparticles [31]. Surface modification by mutagenesis has allowed the production of noble metal nanoparticles within the ferritin interior [32]. Co-crystallisation of metals and semi-conducting compounds has also been explored [12].
Ferritin iron uptake and release in the presence of metals and metalloproteins: Chemical implications in the brain
2013, Coordination Chemistry ReviewsCitation Excerpt :Different studies provide evidence that metal cations are bound by ferritin [28] usually in two separate types of sites of very different binding constants. These two classes of binding sites are localized either within the cavity or at the external shell [28]. Interestingly, the largest number of binding sites is for divalent metal cations, although some of them are functional and others are nonspecific and do not play any decisive role in the genuine properties of ferritin.
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This research was supported by Research Grant 5R01 DK36799-05 from the National Institutes of Health.
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SP, BW, and CL were partially supported by the Undergraduate Research Program of the College of Physical and Mathematical Sciences at Brigham Young University.