Ferritin as an iron-storage protein: mechanisms of iron uptake

1986 ◽  
Vol 27 (4) ◽  
pp. 287-293 ◽  
Author(s):  
Pauline M. Harrison ◽  
Amyra Treffry ◽  
Terence H. Lilley
Keyword(s):  
Storage Protein ◽  
Iron Uptake ◽  
Iron Storage ◽  
Iron Storage Protein

Analysis of Iron in Ferritin, the Iron-Storage Protein: A General Chemistry Experiment

1998 ◽  
Vol 75 (4) ◽  
pp. 437 ◽  
Author(s):  
Maureen J. Donlin ◽  
Regina F. Frey ◽  
Christopher Putnam ◽  
Jody Proctor ◽  
James K. Bashkin
Keyword(s):  
General Chemistry ◽  
Storage Protein ◽  
Protein A ◽  
Iron Storage ◽  
Chemistry Experiment ◽  
Iron Storage Protein

scholarly journals Preparation of platinum nanoparticles using iron(ii) as reductant and photosensitized H2 generation on an iron storage protein scaffold

RSC Advances ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 5551-5559
Author(s):  
Brenda S. Benavides ◽  
Silvano Valandro ◽  
Donald M. Kurtz
Keyword(s):  
Heavy Chain ◽  
Platinum Nanoparticles ◽  
Storage Protein ◽  
Iron Storage ◽  
Protein Scaffold ◽  
H2 Generation ◽  
Iron Storage Protein

An assembly of platinum nanoparticles produced by Fe(ii) reduction of Pt(ii) and stabilized by human heavy chain ferritin's native catalysis of Fe(ii)(aq) autoxidation functions as an efficient photosensitized H2 evolution catalyst.

scholarly journals Ferritin does not accumulate iron oxidized by caeruloplasmin

1995 ◽  
Vol 305 (1) ◽  
pp. 21-23 ◽  
Author(s):  
A Treffry ◽  
D Gelvan ◽  
A M Konijn ◽  
P M Harrison
Keyword(s):  
Dissolved Oxygen ◽  
Storage Protein ◽  
Iron Oxidation ◽  
Primary Effect ◽  
Significant Extent ◽  
Iron Storage ◽  
Horse Spleen Ferritin ◽  
Iron Storage Protein

Ferritin is an iron-storage protein ubiquitous in mammals, plants and bacteria. It can be reconstituted, in vitro, from the apoprotein and Fe(II) salts in the presence of dissolved oxygen. Recently it has been reported that caeruloplasmin can facilitate apoferritin reconstitution and that iron oxidized by caeruloplasmin is sequestered within the ferritin shell. Here we show that the primary effect of adding caeruloplasmin to horse spleen ferritin during reconstitution is the competition between the two molecules for the iron. This competition results in overall increased rates of iron oxidation and a mixture of products, namely iron-containing ferritin and iron hydroxy polymers attached to caeruloplasmin. Iron oxidized by caeruloplasmin is not incorporated, to any significant extent, into horse spleen ferritin.

Increased Expression of Ferritin, an Iron-storage Protein, in Specific Regions of the Parahippocampal Cortex of Epileptic Rats

Epilepsia ◽  
2005 ◽  
Vol 46 (9) ◽  
pp. 1371-1379 ◽  
Author(s):  
Jan A. Gorter ◽  
Ana R.M. Mesquita ◽  
Erwin A. van Vliet ◽  
Fernando H. Lopes da Silva ◽  
Eleonora Aronica
Keyword(s):  
Storage Protein ◽  
Iron Storage ◽  
Parahippocampal Cortex ◽  
Iron Storage Protein

Intracellular Sequestration of223Ra by the Iron-Storage Protein Ferritin

2005 ◽  
Vol 164 (2) ◽  
pp. 230-233 ◽  
Author(s):  
Michael J. Atkinson ◽  
Marianne T. Spanner ◽  
Michael Rosemann ◽  
Utz Linzner ◽  
Walter A. Müller ◽  
...  
Keyword(s):  
Storage Protein ◽  
Iron Storage ◽  
Intracellular Sequestration ◽  
Iron Storage Protein

scholarly journals How Does Iron Storage Protein Ferritin Interact with Plutonium (and Thorium)?

2020 ◽  
Author(s):  
Cyril Zurita ◽  
Satoru Tsushima ◽  
Carole Bresson ◽  
Marta Garcia Cortes ◽  
Pier Lorenzo Solari ◽  
...  
Keyword(s):  
Storage Protein ◽  
Iron Storage ◽  
Iron Storage Protein

Long-range solid-state electron transport through ferritin multilayers

2019 ◽  
Vol 7 (29) ◽  
pp. 9038-9048 ◽  
Author(s):  
Sudipta Bera ◽  
Jayeeta Kolay ◽  
Pallabi Pramanik ◽  
Anirban Bhattacharyya ◽  
Rupa Mukhopadhyay
Keyword(s):  
Solid State ◽  
Electron Transport ◽  
Long Range ◽  
Storage Protein ◽  
Solid State Electron ◽  
Iron Storage ◽  
State Electron ◽  
Iron Storage Protein

We have developed a purely protein-based multilayered semiconducting 3D material using iron-storage protein ferritin. It is electronically homogeneous; capable of long range electron transport having a long exciton radius, and showsz-confinement.

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