A synthetic redox biofilm made from metalloprotein–prion domain chimera nanowires - Archive ouverte HAL
Article Dans Une Revue Nature Chemistry Année : 2017

A synthetic redox biofilm made from metalloprotein–prion domain chimera nanowires

Chantal Gondran
Alan Le Goff

Résumé

Engineering bioelectronic components and set-ups that mimic natural systems is extremely challenging. Here we report the design of a protein-only redox film inspired by the architecture of bacterial electroactive biofilms. The nanowire scaffold is formed using a chimeric protein that results from the attachment of a prion domain to a rubredoxin (Rd) that acts as an electron carrier. The prion domain self-assembles into stable fibres and provides a suitable arrangement of redox metal centres in Rd to permit electron transport. This results in highly organized films, able to transport electrons over several micrometres through a network of bionanowires. We demonstrate that our bionanowires can be used as electron-transfer mediators to build a bioelectrode for the electrocatalytic oxygen reduction by laccase. This approach opens opportunities for the engineering of protein-only electron mediators (with tunable redox potentials and optimized interactions with enzymes) and applications in the field of protein-only bioelectrodes.
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Dates et versions

hal-01546112 , version 1 (23-06-2017)

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Lucie Altamura, Christophe Horvath, Saravanan Rengaraj, Anäelle Rongier, Kamal Elouarzaki, et al.. A synthetic redox biofilm made from metalloprotein–prion domain chimera nanowires. Nature Chemistry, 2017, 9 (2), pp.157-163. ⟨10.1038/nchem.2616⟩. ⟨hal-01546112⟩
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