Interprotein electron transfer between FeS-protein nanowires and oxygen-tolerant NiFe hydrogenase

Saravanan Rengaraj (1, 2) , Raoudha Haddad (2) , Elisabeth Lojou (3) , Nicolas Duraffourg (1) , Michael Holzinger (2) , Alan Le Goff (2) , Vincent Forge (1)

1 LCBM - UMR 5249 - Laboratoire de Chimie et Biologie des Métaux
2 DCM - Département de Chimie Moléculaire
3 BIP - Bioénergétique et Ingénierie des Protéines

Self-assembled redox protein nanowires have been exploited as efficient electron shuttles for an oxygen-tolerant hydrogenase. An intra/inter-protein electron transfer chain has been achieved between the iron-sulfur centres of rubredoxin and the FeS cluster of [NiFe] hydrogenases. [NiFe] Hydrogenases entrapped in the intricated matrix of metalloprotein nanowires achieve a stable, mediated bioelectrocatalytic oxidation of H2 at low-overpotential.

Keywords: protein nanowires; biofuel cells; amyloid fibers; H-2 oxidation; hydrogenases

Domains: Chemical Sciences; Chemical Sciences; Catalysis; Life Sciences [q-bio]

Saravanan Rengaraj, Raoudha Haddad, Elisabeth Lojou, Nicolas Duraffourg, Michael Holzinger, et al.. Interprotein electron transfer between FeS-protein nanowires and oxygen-tolerant NiFe hydrogenase. Angewandte Chemie International Edition, 2017, 56 (27), pp.7774-7778. ⟨10.1002/anie.201702042⟩. ⟨hal-01521959⟩