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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
A reversible proton relay process mediated by hydrogen-bonding interactions in [FeFe]hydrogenase modeling
Kai-Ti Chu1,2,3, Yu-Chiao Liu1, Yi-Lan Huang1
1Institute of Chemistry, Academia Sinica, Nankang, Taipei 115 (Taiwan).
Abstract:
A reversible and temperature-dependent proton-relay process is demonstrated for a Fe2 complex possessing a terminal thiolate in the presence of nitrogen-based acids. The terminal sulfur site (S(t) ) of the complex forms a hydrogen-bond interaction with N,N-dimethylanilinium acid at 183 K. The Fe2 core, instead, is protonated to generate a bridging hydride at 298 K. Reversibility is observed for the tautomerization between the hydrogen-bonded pair and the Fe-hydride species. X-ray structural analysis of the hydrogen-bonded species at 193 K reveals a short N(H)⋅⋅⋅S(t) contact. Employment of pyridinium acid also results in similar behavior, with reversible proton-hydride interconversion. DFT investigation of the proton-transfer pathways indicates that the pKa value of the hydrogen-bonded species is enhanced by 3.2 pKa units when the temperature is decreased from 298 K to 183 K.
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