Literature DB >> 28489268

Interprotein Electron Transfer between FeS-Protein Nanowires and Oxygen-Tolerant NiFe Hydrogenase.

Saravanan Rengaraj1,2, Raoudha Haddad2, Elisabeth Lojou3, Nicolas Duraffourg1, Michael Holzinger2, Alan Le Goff2, Vincent Forge1.   

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.
© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Entities:  

Keywords:  H2 oxidation; amyloid fibers; biofuel cells; hydrogenases; protein nanowires

Mesh:

Substances:

Year:  2017        PMID: 28489268     DOI: 10.1002/anie.201702042

Source DB:  PubMed          Journal:  Angew Chem Int Ed Engl        ISSN: 1433-7851            Impact factor:   15.336


  2 in total

1.  Molecular assemblies built with the artificial protein Pizza.

Authors:  Jeroen P M Vrancken; Jana Aupič; Christine Addy; Roman Jerala; Jeremy R H Tame; Arnout R D Voet
Journal:  J Struct Biol X       Date:  2020-05-28

Review 2.  Optimized Metal Chalcogenides for Boosting Water Splitting.

Authors:  Jie Yin; Jing Jin; Honghong Lin; Zhouyang Yin; Jianyi Li; Min Lu; Linchuan Guo; Pinxian Xi; Yu Tang; Chun-Hua Yan
Journal:  Adv Sci (Weinh)       Date:  2020-04-06       Impact factor: 16.806

  2 in total

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