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Updated: Dec 14, 2025
![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
Identifying a Real Catalyst of [NiFe]-Hydrogenase Mimic for Exceptional H2 Photogeneration
Xu-Zhe Wang1,2, Shu-Lin Meng1,2, Hongyan Xiao3
1Key Laboratory of Photochemical Conversion and Optoelectronic Materials, Technical Institute of Physics and Chemistry, Chinese Academy of Sciences, Beijing, 100190, China.
Abstract:
Inspired by the natural [NiFe]-H2 ase, we designed mimic 1, (dppe)Ni(μ-pdt)(μ-Cl)Ru(CO)2 Cl to realize effective H2 evolution under photocatalytic conditions. However, a new species 2 was captured in the course of photo-, electro-, and chemo- one-electron reduction. Experimental studies of in situ IR spectroscopy, EPR, NMR, X-ray absorption spectroscopy, and DFT calculations corroborated a dimeric structure of 2 as a closed-shell, symmetric structure with a RuI center. The isolated dimer 2 showed the real catalytic role in photocatalysis with a benchmark turnover frequency (TOF) of 1936 h-1 for H2 evolution, while mimic 1 worked as a pre-catalyst and evolved H2 only after being reduced to 2. The remarkably catalytic activity and unique dimer structure of 2 operated in photocatalysis unveiled a broad research prospect in hydrogenases mimics for advanced H2 evolution.
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