Multiple Proton Translocation Paths Reveal a Novel Function of Ferritin as a Source of Protons for Cellular Metabolism

Ferritin stores iron as Fe[Formula: see text] after being oxidized in the presence of molecular oxygen. The Fe[Formula: see text] ions typically enter into the ferroxidase as hexahydrate, where the oxidation of Fe[Formula: see text]to Fe[Formula: see text] 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 [Formula: see text]-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[Formula: see text] to Fe[Formula: see text], 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.

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Publication Details

Journal
Journal of Computational Biophysics and Chemistry
Published
2024-08-23
DOI
https://doi.org/10.1142/s2737416524500467
Citations
1
Primary Topic
Metabolism and Genetic Disorders
Type
article
Field-Weighted Citation Impact
0.38

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article

Multiple Proton Translocation Paths Reveal a Novel Function of Ferritin as a Source of Protons for Cellular Metabolism

Shivani R. Nandha, Chandrasekaran Palaniappan, Rahul Checker, D. Vaigundan
1 citations
Journal of Computational Biophysics and Chemistry
Metabolism and Genetic Disorders
0.38
article

Multiple Proton Translocation Paths Reveal a Novel Function of Ferritin as a Source of Protons for Cellular Metabolism

Shivani R. Nandha, Chandrasekaran Palaniappan, Rahul Checker, D. Vaigundan
article en
1 citations

Abstract

Ferritin stores iron as Fe[Formula: see text] after being oxidized in the presence of molecular oxygen. The Fe[Formula: see text] ions typically enter into the ferroxidase as hexahydrate, where the oxidation of Fe[Formula: see text]to Fe[Formula: see text] 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 [Formula: see text]-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[Formula: see text] to Fe[Formula: see text], 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.

Journal of Computational Biophysics and ChemistryVol. 24(01)
Bhabha Atomic Research Centre (IN), Homi Bhabha National Institute (IN), Indian Institute of Science Bangalore (IN)
Bhabha Atomic Research Centre
Zero hunger
Openalex Percentile: Top 37%
Metabolism and Genetic Disorders
0.38
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Multiple Proton Translocation Paths Reveal a Novel Function of Ferritin as a Source of Protons for Cellular Metabolism — Shivani R. Nandha, Chandrasekaran Palaniappan, et al. · Journal of Computational Biophysics and Chemistry (2024) | TGRS Research Map | TGRS