Interprotein Electron Transfer between FeS‐Protein Nanowires and Oxygen‐Tolerant NiFe Hydrogenase. Issue 27 (6th June 2017)

• Record Type: Journal Article
• Authors: Rengaraj, Saravanan; Haddad, Raoudha; Lojou, Elisabeth; Duraffourg, Nicolas; Holzinger, Michael; Le Goff, Alan; Forge, Vincent
• Is Part Of: Angewandte Chemie international edition. Volume 56:Issue 27(2017)
• Page Start: 7774
• Page End: 7778
• Publication Date: 2017-06-06
• Subjects: amyloid fibers -- biofuel cells -- H2 oxidation -- hydrogenases -- protein nanowires; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201702042
• Languages: English
• ISSNs: 1433-7851

Abstract

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 centers 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. Abstract : Wired up : Self‐assembled redox protein nanowires were exploited as efficient electron shuttles for an oxygen‐tolerant hydrogenase. [NiFe] Hydrogenases entrapped in the intricate matrix of metalloprotein nanowires achieve a stable, mediated bioelectrocatalytic oxidation of H2 at low overpotential.