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![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
Fe-S complexes containing five-membered heterocycles: novel models for the active site of hydrogenases with unusual
Shi Jiang1, Jianhui Liu, Yu Shi
1State Key Laboratory of Fine Chemicals, DUT-KTH Joint Education and Research Center on Molecular Devices, Dalian University of Technology (DUT), Zhongshan Road 158-40, Dalian, 116012, P. R. China.
Abstract:
Three biomimetic 2Fe2S complexes [{(micro-SCH2)2NCH2(2-C4H3O)}](Fe2(CO)6), [{(micro-SCH2)2 NCH2(2-C4H3S)}](Fe2(CO)6) and [{(micro-SCH2)2NCH2(5-Br-2-C4H2S)}Fe2(CO)6] were prepared as models for the active site of Fe-only hydrogenase by the convergent process from [(micro-S2)Fe2(CO)6] and N,N-bis(hydromethyl)-2-furan and thiophene. The structures of these complexes were identified spectroscopically and crystallographically. The electrochemical behavior of the complexes and was unique as they showed catalytic proton reduction with a low reduction potential at -1.13 and -1.09 V vs Fc/Fc+, respectively, in the presence of HClO4.
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