Water oxidation by Ferritin: A semi-natural electrode
Zahra Abdi1, Robabeh Bagheri2, Zhenlun Song2
1Department of Chemistry, Institute for Advanced Studies in Basic Sciences (IASBS), Zanjan, 45137-66731, Iran.
Abstract:
Ferritin is a protein (ca. 12 nm) with a central pocket of 6 nm diameter, and hydrated iron oxide stored in this central cavity of this protein. The protein shell has a complicated structure with 24 subunits. Transmission electron microscopy images of ferritin showed nanosized iron oxides (ca. 4-6 nm) in the protein structure. In high-resolution transmission electron microscopy images of the iron core, d-spacings of 2.5-2.6 Å were observed, which is corresponded to d-spacings of ferrihydrite crystal structure. Our experiments showed that at pH 11, the modified electrode by this biomolecule is active for water oxidation (turnover frequency: 0.001 s-1 at 1.7 V). Using affected by bacteria, we showed that Fe ions in the structure of ferritin are critical for water oxidation.
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