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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
Mechanism of hydrogen evolution catalyzed by NiFe hydrogenases: insights from a Ni-Ru model compound
Loredana Vaccaro1, Vincent Artero, Sigolène Canaguier
1Laboratoire de Dynamique Moléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, UMR CNRS/UJF/CEA 5075, 41 rue Jules Horowitz F-38027, Grenoble cedex 1, France.
Abstract:
DFT modeling has been used to investigate a previously proposed mechanism of proton reduction catalyzed by [Ni(xbsms)Ru(CO)(2)Cl(2)] (H(2)xbsms = 1,2-bis(4-mercapto-3,3-dimethyl-2-thiabutyl)benzene), a bio-inspired mimic of NiFe hydrogenases based on a Ni-Ru framework. Protonation of the 2e(-)-reduced compound, from which a chloride anion has been eliminated, results in the formation of a semi-bridging hydride derivative with structural features comparable to those of the Ni-C state catalytic intermediate of native hydrogenases. The present study thus provides structural and functional insights into the enzymatic mechanism including the possible involvement of a bridging hydride derivative and heterolytic formation of a dihydrogen molecule on a {Ni(mu-S)(2)M} framework.
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