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Tailor‐Made Modification of a Gold Surface for the Chemical Binding of a High‐Activity [FeFe] Hydrogenase
Author(s) -
Krassen Henning,
Stripp Sven T.,
Böhm Nadine,
Berkessel Albrecht,
Happe Thomas,
Ataka Kenichi,
Heberle Joachim
Publication year - 2011
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.201001190
Subject(s) - hydrogenase , chemistry , redox , photochemistry , electron transfer , catalysis , combinatorial chemistry , inorganic chemistry , linker , electrochemistry , hydride , electrode , hydrogen , organic chemistry , computer science , operating system
Hydrogenases are iron–sulfur proteins that catalyze hydrogen turnover in a wide range of microorganisms. Three different classes have been described, and among these [FeFe] hydrogenases are the most active in H 2 evolution. Hydrogenases are redox enzymes that have been shown to exchange electrons with graphite and modified noble metal electrodes. Making use of the latter, diffusible electron carriers are required to enable redox catalysis, as proteins do not specifically bind to the electrode surface. Diffusion‐limited electron transfer can be replaced by electron injection into immobilized hydrogenase by binding the redox mediator to the electrode surface. Here, we present the synthesis and spectroelectrochemical characterization of 1‐(10‐mercaptodecyl)‐1′‐benzyl‐4,4′‐bipyridinium dibromide (MBBP), which is used as redox‐active linker. Cr HydA1, the high‐activity [FeFe] hydrogenase from Chlamydomonas reinhardtii , is immobilized on the linker‐modified gold electrode. Each surface modification step is controlled in situ by surface‐enhanced infrared absorption spectroscopy (SEIRAS). Functionality of the electrode–protein hybrid is demonstrated by recording the linker‐supported current. The specificcatalytic rate of hydrogen evolution by Cr HydA1 (2.9 μmol H 2 min –1 mg –1 hydrogenase) promises a valuable approach for further optimization of this novel bioelectrical interface.