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

Lucie Altamura, Christophe Horvath, Saravanan Rengaraj, Anaëlle Rongier, Kamal Elouarzaki, Chantal Gondran, Anthony L B Maçon, Charlotte Vendrely, Vincent Bouchiat, Marc Fontecave, Denis Mariolle, Patrice Rannou, Alan Le Goff, Nicolas Duraffourg, Michael Holzinger, Vincent Forge

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40 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)157-163
Number of pages7
JournalNature Chemistry
Issue number2
Early online date10 Oct 2016
Publication statusPublished - 1 Feb 2017

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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    Altamura, L., Horvath, C., Rengaraj, S., Rongier, A., Elouarzaki, K., Gondran, C., Maçon, A. L. B., Vendrely, C., Bouchiat, V., Fontecave, M., Mariolle, D., Rannou, P., Le Goff, A., Duraffourg, N., Holzinger, M., & Forge, V. (2017). A synthetic redox biofilm made from metalloprotein-prion domain chimera nanowires. Nature Chemistry, 9(2), 157-163. https://doi.org/10.1038/NCHEM.2616