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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, *
* Corresponding author
1 LCBM - UMR 5249 - Laboratoire de Chimie et Biologie des Métaux
2 DCM - Département de Chimie Moléculaire
3 BIP - Bioénergétique et Ingénierie des Protéines
Abstract : 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 : amyloid fibers biofuel cells H-2 oxidation hydrogenases protein nanowires
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Journal articles
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https://hal-amu.archives-ouvertes.fr/hal-01521959
Contributor : Laure Azzopardi <>
Submitted on : Friday, May 12, 2017 - 3:28:29 PM
Last modification on : Wednesday, October 7, 2020 - 3:14:31 AM

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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, Wiley-VCH Verlag, 2017, 56 (27), pp.7774-7778. ⟨10.1002/anie.201702042⟩. ⟨hal-01521959⟩

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