Premium
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
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201702042
Subject(s) - hydrogenase , overpotential , rubredoxin , electron transfer , nanowire , chemistry , redox , iron–sulfur cluster , electron transport chain , polyoxometalate , metalloprotein , ferredoxin , oxygen , nanotechnology , electrochemistry , crystallography , catalysis , inorganic chemistry , materials science , photochemistry , enzyme , biochemistry , electrode , organic chemistry
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom