scholarly journals Structural, Photophysical, and Photochemical Characterization of Zinc Protoporphyrin IX in a Dimeric Variant of an Iron Storage Protein: Insights into the Mechanism of Photosensitized H2 Generation

2019 ◽  
Vol 123 (31) ◽  
pp. 6740-6749 ◽  
Author(s):  
Brenda S. Benavides ◽  
Rajendra Acharya ◽  
Emily R. Clark ◽  
Priyanka Basak ◽  
Michael J. Maroney ◽  
...  
Keyword(s):  
Storage Protein ◽  
Protoporphyrin Ix ◽  
Zinc Protoporphyrin ◽  
Iron Storage ◽  
H2 Generation ◽  
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 Characterization of nuclear ferritin and mechanism of translocation

2005 ◽  
Vol 388 (3) ◽  
pp. 731-740 ◽  
Author(s):  
Nodar SURGULADZE ◽  
Stephanie PATTON ◽  
Anna COZZI ◽  
Michael G. FRIED ◽  
James R. CONNOR
Keyword(s):  
Storage Protein ◽  
Potent Inhibitor ◽  
Nuclear Volume ◽  
Cell Nuclei ◽  
Iron Depletion ◽  
Iron Storage ◽  
Astrocytoma Cells ◽  
Established Fact ◽  
Iron Storage Protein

Ferritin, normally considered a cytoplasmic iron-storage protein, is also found in cell nuclei. It is an established fact that H-ferritin is the major form of nuclear ferritin, but little is known about the roles of ferritin in nuclei or about the mechanisms that control its appearance within the nuclear volume. In the present study, we show that, for human SW1088 astrocytoma cells, the nuclear and cytoplasmic forms of H-ferritin are products of the same mRNA. Histochemical and biochemical evidence is presented showing that ferritin is distributed non-randomly within the nuclear volume and that it preferentially associates with heterochromatin. Both cytoplasmic and nuclear populations of H-ferritin contain mixtures of non- and O-glycosylated forms, but the nuclear population is enriched in O-glycosylated forms. Cells treated with alloxan, a potent inhibitor of O-glycosylation, contained significantly less nuclear ferritin compared with cells grown in control media. Alloxan inhibited the reappearance of H-ferritin in nuclei of cells released from conditions of iron depletion, but did not prevent its disappearance from nuclei of cells undergoing iron depletion. These results suggest that O-glycosylation accompanies the transfer of ferritin from the cytoplasm to the nucleus, but does not influence the reverse process. The picture that emerges is one in which ferritin translocation between the cytoplasm and the nucleus is post-translationally regulated and responds to environmental and nutritional cues.

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 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.

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

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
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