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Hybrid Amyloid‐Based Redox Hydrogel for Bioelectrocatalytic H 2 Oxidation
Author(s) -
Duraffourg Nicolas,
Leprince Maxime,
Crouzy Serge,
Hamelin Olivier,
Usson Yves,
Signor Luca,
Cavazza Christine,
Forge Vincent,
Albertin Luca
Publication year - 2021
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.202101700
Subject(s) - redox , overpotential , chemistry , moiety , electron transfer , hydrogenase , catalysis , electrode , polymer chemistry , combinatorial chemistry , photochemistry , electrochemistry , inorganic chemistry , organic chemistry
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 H 2 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.