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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
Critical aspects of [NiFe]hydrogenase ligand composition
Koji Ichikawa1, Takahiro Matsumoto, Seiji Ogo
1Center for Future Chemistry, Kyushu University, Nishi-ku, Fukuoka, Japan.
Abstract:
Structural analysis of the resting state of [NiFe]hydrogenase ([NiFe]H(2)ase) shows that the active site has a characteristic bis(mu-thiolato)NiFe unit, where the Ni atom and the Fe atom are bridged by an undetermined oxygen-bearing ligand. This ligand probably derives from the aqueous solvent and is therefore most likely to be H(2)O, OH(-) or O(2-). Here, we compare the reactivities of a NiFe and a NiRu complex when bearing either acetonitrile or aqueous ligands and demonstrate the critical role of an aqueous ligand in hydrogenase and its mimics. We also make observations on the necessity of organometallic metal-carbon bonds to the supporting frameworks.
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