Metal ion binding to apo, holo, and reconstituted horse spleen ferritin

Pead, S.; Durrant, E.; Webb, Bruce A.; Larsen, Christopher A.; Heaton, Duane E.; Johnson, Joseph L.; Watt, Gerald D.

doi:10.1016/0162-0134(94)00050-k

Cited by 67 publications

(73 citation statements)

References 20 publications

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“…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].…”

Section: Cadmium(ii) Concentrates Preferentially Around the Entry Of mentioning

confidence: 99%

“…Ferritin can bind or accommodate metal ions other than Fe in several types of binding sites [27,28]. More importantly, the disruption of the ferritin function in iron uptake or iron release is influenced by the presence of some metals [29], some metalloproteins [30,31], and some other types of biomolecule.…”

Section: Fig 1 Horse Spleen Ferritin Structure: a 24-subunit Oligommentioning

confidence: 99%

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Ferritin iron uptake and release in the presence of metals and metalloproteins: Chemical implications in the brain

Carmona

Palacios

Gálvez

et al. 2013

Coordination Chemistry Reviews

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Living organisms have developed a chemical machinery based on the ferritin protein for the storage, under a nontoxic form, of the iron that is not required for immediate metabolic purposes. Whereas free iron causes extensive cell damage, ferritin iron is not toxic, yet still available for cell requirements. However, iron storage in ferritin is increasingly being recognized as a crucial process related with some neurodegenerative disorders and therefore, an understanding of the management of iron in the brain, especially the processes of iron uptake and release in ferritin, is compulsory to clarify the role of this metalloprotein in these neuropathologies.Although knowledge of iron storage and iron release in ferritin is nowadays still limited, even less information is currently available about the influence of free metal ions and other brain metalloproteins in these processes.In this sense, this review is an excellent opportunity to collect all the information today available about the influence of metals and metalloproteins in ferritin loading and unloading events, which until now are dispersed in the literature.Furthermore, we will focus on the importance of all the above-mentioned interactions in the brain, since the importance of the correct and safe balance of metals in the brain after their well-known implication in neurodegenerative 52 processes such as the lzheimer's ( ), Parkinson (P ) and prion protein (PP ) diseases is obvious. In this work, we will not only recall the importance and role of ferritin in the brain but also the putative influence of the interaction between ferritin and some metals and/or metalloproteins and other biomolecules on these neurological dysfunctions. The final part of the review will be devoted to draw some guidelines to where the future prospects point to on the basis of the existing information.

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Section: Cadmium(ii) Concentrates Preferentially Around the Entry Of mentioning

confidence: 99%

Section: Fig 1 Horse Spleen Ferritin Structure: a 24-subunit Oligommentioning

confidence: 99%

Ferritin iron uptake and release in the presence of metals and metalloproteins: Chemical implications in the brain

Carmona

Palacios

Gálvez

et al. 2013

Coordination Chemistry Reviews

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“…[9] Native apoferritin consists of a spherical protein shell surrounding an aqueous cavity of about 8 nm. [10] It was reported that apoferritin binds or concentrates metal ions in its cavity [11] and that, interestingly, the loaded metal ions can be chemically reduced to form the corresponding zero-valent cluster, which remains encapsulated. [12] Moreover other inorganic nanoparticles (especially oxides and hydroxides) can be prepared within the apoferritin cavity by using different strategies.…”

Section: Introductionmentioning

confidence: 99%

Size‐Controlled Water‐Soluble Ag Nanoparticles

et al. 2007

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Ag nanoparticles of two different sizes (1 and 4 nm) were prepared within an apoferritin cavity by using an Ag+‐loaded apoferritin as a nanoconfined environment for their construction. The initial amount of Ag+ ions injected in the apoferritin cavity dictates the size of the final Ag particles. The protein shell prevents bulk aggregation of the metal particles, which renders them water soluble and extremely stable.(© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2007)

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“…Moreover, redox-active metal ions can be synthesised in apoferritin with the most satisfying results found for Mn(II), which can create amorphous manganese oxide cores [68]. Other bivalent metal ions like Cd 2+ bind to the apoferritin cavity and thus can be used for the reconstruction of semiconductor NPs inside apoferritin [67,69]. QDs and nucleated nanoscale CdS crystallites within the apoferritin cavity, created by the reaction of Cd 2+ and HS -, can offer unique photoresponsive and photoredox properties.…”

Section: Synthesis Of Nanoparticles Within the Apoferritin Cagementioning

confidence: 99%

“…Firstly, positive metal ions need to be introduced to the demetallated protein cavity (apoferritin) and condensed at nucleation sites, which after the addition of anions encourages nucleation. Anion induction in the cavity should also be faster than chemical reactions outside [69].…”

Section: Synthesis Of Nanoparticles Within the Apoferritin Cagementioning

confidence: 99%