Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1947950 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2010 | 13 Pages |
Abstract
The ferritin 3-fold channels are shown to be flexible structures that allow the entry and exit of different ions and molecules through the protein shell. The H- and L-subunits are shown to have complementary roles in iron oxidation and mineralization, and hydrogen peroxide appears to be a by-product of oxygen reduction at the FC of most ferritins. The di-iron(III) complex at the FC of some ferritins acts as a stable cofactor during iron oxidation rather than a catalytic center where Fe(II) is oxidized at the FC followed by its translocation to the protein cavity.
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Authors
Fadi Bou-Abdallah,