Hybrid Amyloid-Based Redox Hydrogel for Bioelectrocatalytic H2 Oxidation
Résumé
An artificial amyloid-based redox hydrogel was designed for mediating electron transfer between a [NiFeSe] hydrogenase and an electrode. Starting from a mutated prion-forming domain of fungal protein HET-s, a hybrid redox protein containing a single benzyl methyl viologen moiety was synthesized. This protein was able to self-assemble into structurally homogenous nanofibrils. Molecular modeling confirmed that the redox groups are aligned along the fibril axis and are tethered to its core by a long, flexible polypeptide chain that allows close encounters between the fibril-bound oxidized or reduced redox groups. Redox hydrogel films capable of immobilizing the hydrogenase under mild conditions at the surface of carbon electrodes were obtained by a simple pH jump. In this way, bioelectrodes for the electrocatalytic oxidation of H2 were fabricated that afforded catalytic current densities of up to 270 μA cm−2, with an overpotential of 0.33 V, under quiescent conditions at 45 °C.
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2021_ACIE_BMV-HET_NiFeSeHyDB_Preprint_v1.pdf (2.43 Mo)
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anie202101700-s1-2021_acie_bmv-het_nifesehydb_supporting_information_v1.pdf (4.64 Mo)
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