<▼1>
Ferritin stores iron as Fe$ ^{3+}$ after being oxidized in the presence of molecular oxygen. The Fe$ ^{2+}$ ions typically enter into the ferroxidase as hexahydrate, where the oxidation of Fe$ ^{2+}$to Fe$ ^{3+}$ occurs. The studies predict probable residues involved in the entry of molecular oxygen by sequence and structural comparison with other proteins. This study identified the probable $ \pi $-H paths for electron transfer and proton translocation in ferritin through structural analysis. The identification of multiple proton translocation paths and the use of hexahydrate iron as substrate by ferritin indicate that during the oxidation of Fe$ ^{2+}$ to Fe$ ^{3+}$, all the water molecules of iron may be utilized. The resulting byproducts, protons and hydroxyl ions may be one of the sources for the proton gradient required to drive oxidative phosphorylation by electron transport complexes in mitochondria. Also, it may be required to acidify lysosomes and generate nitroperoxy species.
<▼2>
Comparative sequence analysis, structural analysis, and molecular dynamics simulation identified the likely route of molecular oxygen entry in ferritin
Structural analysis of ferritin invoked several hydrogen bond networks likely involved in proton translocation paths
Iron hexahydrate as a substrate instead of simple iron in the ferritin-catalyzed reaction is implicated as a source of protons to maintain the mitochondrial membrane potential and intuitively other cellular needs
- Book : 24(1)
- Pub. Date : 2025
- Page : pp.53-65
- Keyword :
