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Interprotein Electron Transfer between FeS‐Protein Nanowires and Oxygen‐Tolerant NiFe Hydrogenase
Author(s) -
Rengaraj Saravanan,
Haddad Raoudha,
Lojou Elisabeth,
Duraffourg Nicolas,
Holzinger Michael,
Le Goff Alan,
Forge Vincent
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201702042
Subject(s) - electron transfer , nanowire , hydrogenase , chemistry , electron , oxygen , nanotechnology , materials science , catalysis , biochemistry , photochemistry , physics , organic chemistry , quantum mechanics
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 H 2 at low‐overpotential.
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