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Updated: May 2, 2026
![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
Stabilization of a Terminal Hydride Through Regioselective Protonation in a Diiron Complex Inspired by
Lucile Chatelain1, Sven T Stripp2, Philippe Schollhammer1
1UMR CNRS 6521 Chimie, Electrochimie Moléculaires et Chimie Analytique, Univ. Brest, 6 Avenue Victor le Gorgeu, CS93837, Brest-Cedex 3, 29238, France.
Abstract:
Protonation studies of the complex [Fe2(μ-pdt)(κ2-dmpe)2(CO)2] (1), inspired by the [FeFe]-hydrogenases active site cofactor, yield terminal and bridging hydrido isomers in a ratio that depends on the acid strength and steric hindrance. A terminal hydride ligand is mainly obtained in presence of weaker acids such as [HPtBu3][BF4] and [HNEt3][BF4] while a bridging isomer is predominantly formed with stronger acids such as [HPPh3][BF4] and [H(OEt2)][BF4]. The terminal isomer is comparatively stable and undergoes isomerization into the bridging hydride following first-order kinetics, with half-lives of 21 days and 3 days at room temperature and 40 °C, respectively.
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