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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
Unusual formation of a [NiSFe(2)(CO)(6)] cluster: a structural model for the inactive form of [NiFe] hydrogenase
Alessandro Perra1, Qiang Wang, Alexander J Blake
1University of Nottingham, Nottingham, UKNG7 2RD.
Abstract:
The synthesis and characterisation of the trinuclear Ni-Fe complex [Ni(L(2))SFe(2)(CO)(6)] (1) formed from the reaction of [Ni(L(1))] with Fe(3)(CO)(12) is described. The single-crystal X-ray structure of 1 shows Ni(ii) bound to three thioether R(2)-S donors and bridged by a sulfide (S(2-)) group to two Fe(CO)(3) units. undergoes a reversible one-electron reduction process at E(1/2) = -1.62 V vs. Fc(+)/Fc to generate 1 (-), which has been characterised by UV-vis and IR spectroelectrochemistry and by EPR spectroscopy. DFT calculations on 1and 1 (-) reveal electronic structures that are delocalised across the NiFe(2) core. The SOMO in 1 (-) possesses Ni-Fe and Fe-Fe anti-bonding character and lies approximately in the plane defined by the equilateral triangle of Ni and Fe atoms. It possesses d-orbital contributions of 18.5, 15.0 and 19.8% for the Ni(1), Fe(1) and Fe(2) atoms, respectively. The Ni-S(sulfide) bond length in 1 [2.1654(7) A] is identical to that for the bridging sulfide found in the oxidised inactive form of the [NiFe] hydrogenase from D. vulgaris (2.16 A). Thus, 1 provides a useful comparison for biological [NiFe] centres bridged by sulfide donors.
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