Sonia Levi

TL;DR: The X-ray structure of human H ferritin shows a novel metal site embedded within each of its four-helix bundles and it is suggested that ferroxidase activity associated with this site accounts for its rapid uptake of iron10.

TL;DR: In this article, a new ferritin specific for the mitochondria, which is functionally similar to the H-ferritin, opens new perspectives in the study of the relationships between iron, oxidative damage and free radicals.

TL;DR: An unusual intronless gene on chromosome 5q23.1 is reported that encodes a 242-amino acid precursor of a ferritin H-like protein that accumulates in high amounts in iron-loaded mitochondria of erythroblasts of subjects with impaired heme synthesis and may play an important role in the regulation of mitochondrial iron homeostasis andHeme synthesis.

TL;DR: It is concluded that the ferritin H-chain has an iron oxidation site which is separated from the sites of iron transfer and hydrolysis and that either the integrity of the molecule or the presence of the amino acid sequences forming the hydrophobic channel is necessary for iron core formation.

TL;DR: Comparison of the three-dimensional structures of mammalian and invertebrate ferritins, as well as computer modeling of plant ferritin and of BFR, indicate a well conserved molecular framework.