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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
Synthesis and Electrocatalytic Property of Diiron Hydride Complexes Derived from a Thiolate-Bridged Diiron Complex
Dawei Yang1, Yang Li1, Baomin Wang1
1State Key Laboratory of Fine Chemicals, School of Pharmaceutical Science and Technology, Faculty of Chemical, Environmental and Biological Science and Technology, Dalian University of Technology , 2 Linggong Road, Dalian 116024, P. R. China.
Abstract:
Interaction of a diiron thiolate-bridged complex, [Cp*Fe(μ-η(2):η(4)-bdt)FeCp*] (1) (Cp* = η(5)-C5Me5; bdt = benzene-1,2-dithiolate) with a proton gives an Fe(III)Fe(III) hydride bridged complex, [Cp*Fe(μ-bdt)(μ-H)FeCp*][BF4] (3[BF4]). According to in situ variable temperature (1)H NMR studies, the formation of 3[BF4] was evidenced to occur through a stepwise pathway: protonation occurring at an iron center to produce terminal hydride [Cp*Fe(μ-bdt)(t-H)FeCp*][BF4] (2) and subsequent intramolecular isomerization to bridging hydride 3[BF4]. A one-electron reduction of 3[BF4] by CoCp2 affords a paramagnetic mixed-valent Fe(II)Fe(III) hydride complex, [Cp*Fe(μ-η(2):η(2)-bdt)(μ-H)FeCp*] (4). Further, studies on protonation processes of diruthenium and iron-ruthenium analogues of 1, [Cp*M1(μ-bdt)M2Cp*] (M1 = M2 = Ru, 5; M1 = Fe, M2 = Ru, 8), provide experimental evidence for terminal hydride species at these bdt systems. Importantly, diiron or diruthenium hydride bridged complexes 3[BF4], 7[BF4] and iron-ruthenium heterodinuclear complex 8[PF6] can realize electrocatalytic hydrogen evolution.
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