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Hybrid Amyloid-Based Redox Hydrogel for Bioelectrocatalytic H2 Oxidation

Authors
  • Duraffourg, Nicolas
  • Leprince, Maxime
  • Crouzy, Serge
  • Hamelin, Olivier
  • Husson, Yves
  • Signor, Luca
  • Cavazza, Christine
  • Forge, Vincent
  • Albertin, Luca
Publication Date
Jan 01, 2021
Identifiers
DOI: 10.1002/anie.202101700
OAI: oai:HAL:hal-03241503v1
Source
HAL-INRIA
Keywords
Language
English
License
Unknown
External links

Abstract

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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