Ultrastructure of ferritin and apoferritin: A review

Massover, William H.

doi:10.1016/0968-4328(93)90005-l

Cited by 173 publications

(149 citation statements)

References 308 publications

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“…To produce nano-sized iron oxide particles we utilized the ability of Ferritin to self-assemble and construct a core of iron oxide. Ferritin is the major cellular iron-storage protein and consists of a spherical hollow shell composed of 24 polypeptide subunits and is able to store iron as hydrated iron oxide in the internal cavity 5,6,7 . The inner and outer diameters of the protein shell are about 8 and 12.5 nm, respectively.…”

Section: Introductionmentioning

confidence: 99%

Electronic structure of nanoscale iron oxide particles measured by scanning tunneling and photoelectron spectroscopies

et al. 2005

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We have investigated the electronic structure of nano-sized iron oxide by scanning tunnelling microscopy (STM) and spectroscopy (STS) as well as by photoelectron spectroscopy. Nano particles were produced by thermal treatment of Ferritin molecules containing a self-assembled core of iron oxide. Depending on the thermal treatment we were able to prepare different phases of iron oxide nanoparticles resembling γ-Fe2O3, α-Fe2O3, and a phase which apparently contains both γ-Fe2O3 and α-Fe2O3. Changes to the electronic structure of these materials were studied under reducing conditions. We show that the surface band gap of the electronic excitation spectrum can differ from that of bulk material and is dominated by surface effects.

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Section: Introductionmentioning

confidence: 99%

Electronic structure of nanoscale iron oxide particles measured by scanning tunneling and photoelectron spectroscopies

et al. 2005

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“…In particular, ferritin is composed of a protein coat of about 130 A diameter, surrounding a biomineral core of about 70 A diameter [1]. Hemosiderin is believed to be the result of the autophagic breakdown of ferritin occurring in particular membrane bounded subcellular structures (lysosomes) named "siderosomes" [2].…”

Section: Introductionmentioning

confidence: 99%

“…Mossbauer Spectroscopy [5] and Exended X-ray Absorption Fine Structure analysis (EXAFS) [6]. It has been shown [1], that in both proteins, in human non pathological conditions, the biomineral core is a crystal with a structure based on Fe3+ oxide, like ferrihydrite (SFe203 9H20). Nevertheless, recent investigations clearly show that there are several types of biomineral cores of hemosiderins occurring in different human pathologies [7].…”

Section: Introductionmentioning

confidence: 99%

Electron Energy Loss Spectroscopy Study of Iron Deposition in Human Alveolar Macrophages: Ferritin or Hemosiderin?

Diociaiuti

Falchi

Paoletti

1995

Microsc. Microanal. Microstruct.

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Abstract. 2014 Electron energy loss spectroscopy imaging (EELSI) was used to obtain Fe maps, with molecular resolution, in human alveolar macrophages. Fe concentrations were found in particular structures named siderosomes. The combined application of Extended energy loss fine structure (EX-ELFS) analysis, a "short-range " probe, and Selected area electron diffraction (SAED), a "long-range" probe, allowed us to investigate the atomic arrangement of proteins constituting the siderosomes. Results are compared with structural data obtained on purified proteins. It is found that the siderosomes seem to be constituted mainly by normal hemosiderins.

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confidence: 99%

“…Ferritin H and L subunit ratios are unique to each organ within the human body. H rich ferritins are prominent in organs such as human heart and brain while the L rich ferritins are primarily observed in storage organs such as the liver and spleen [1].Understanding the mechanisms involved in the iron core formation as well the characterization of the iron core structure in ferritin has been a subject of interest from many years. Evidence indicates the association of the iron oxide core composition in dysfunctional ferritins with many neurological and non-neurological diseases such as Alzheimer's disease, Parkinson's disease, Cardiomyopathy, and Hemochromatosis.…”

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Revealing the Iron Oxides Mineral Core in Ferritin due to the Variations in the H and L Subunits

et al. 2017

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Iron is an essential element involved in electron transfer processes in many biological reactions in the human body. Excess iron is stored and regulated in ferritin proteins during the biomineralization and demineralization processes. Cytosolic ferritin is 12nm in diameter and composed of a 24-subunit protein shell containing Heavy (H) and Light (L) chains and a ferritin iron core approximately 8nm in diameter. The H subunits are responsible for iron detoxification while L subunits are responsible for iron storage. Ferritin H and L subunit ratios are unique to each organ within the human body. H rich ferritins are prominent in organs such as human heart and brain while the L rich ferritins are primarily observed in storage organs such as the liver and spleen [1].Understanding the mechanisms involved in the iron core formation as well the characterization of the iron core structure in ferritin has been a subject of interest from many years. Evidence indicates the association of the iron oxide core composition in dysfunctional ferritins with many neurological and non-neurological diseases such as Alzheimer's disease, Parkinson's disease, Cardiomyopathy, and Hemochromatosis. Magnetite and maghemite were the most commonly observed iron oxides in dysfunctional ferritin [3]. Different studies suggest possible reasons for different iron core compositions, which include the rate of biomineralization [2] and demineralization processes [4] and the electron beam effect on the material, which could alter the core structure [5]. To explore the biomineralization and demineralization processes and further understand the formation of different iron oxides, the contribution of H and L subunits needs to be better understood.In the present study, commercially available H rich and the L rich ferritins obtained from healthy human hearts and human spleens were compared. In order to prevent artifacts and electron beam damage, the characterization of the proteins was performed in the native liquid state of the protein by utilization of Graphene Liquid Cells (GLCs). The high electron conductivity of graphene and the ability of GLCs to encapsulate thin liquid samples [6] were implemented to obtain spatially resolved Electron Energy Loss Spectroscopy (EELS) to determine the oxidation states of iron. Selected Area Electron Diffraction (SAED) analyses of the crystal structures were obtained to identify different iron oxides.The studies were carried out with controlled electron dosage at a low electron voltage of 80keV. From EELS data (Figure 1), the ratio of Fe +2 / Fe +3 was 0.24 in human heart ferritin (HHF), indicating the presence of hematite (-Fe2O3). However, the ratio of Fe +2 /Fe +3 was 0.50 in human spleen ferritin (HSF), indicating the presence of magnetite ( Fe +2 Fe +3 2O4) as a major iron oxide in the L rich ferritins. To further characterize the iron oxides of the proteins, SAED (Figure 2) was performed, which indicated the presence of hematite with trace amounts of maghemite (-Fe2O3), ferrihydrite (Fe +3 2O3.O.5H20), and ma...

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Ultrastructure of ferritin and apoferritin: A review

Cited by 173 publications

References 308 publications

Electronic structure of nanoscale iron oxide particles measured by scanning tunneling and photoelectron spectroscopies

Electronic structure of nanoscale iron oxide particles measured by scanning tunneling and photoelectron spectroscopies

Electron Energy Loss Spectroscopy Study of Iron Deposition in Human Alveolar Macrophages: Ferritin or Hemosiderin?

Revealing the Iron Oxides Mineral Core in Ferritin due to the Variations in the H and L Subunits

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