Protonation of [FeFe]-hydrogenase sub-site analogues: revealing mechanism using FTIR stopped-flow techniques

Wright, Joseph A. ORCID: https://orcid.org/0000-0001-9603-1001, Webster, Lee, Jablonskytė, Aušra, Woi, Pei Meng, Ibrahim, Saad and Pickett, Christopher J (2011) Protonation of [FeFe]-hydrogenase sub-site analogues: revealing mechanism using FTIR stopped-flow techniques. Faraday Discussions, 148. pp. 359-371.

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Abstract

The formation of transient metal hydride(s) at the metallo-sulfur active sites of [FeFe]-hydrogenase is implicated in both hydrogen evolution and uptake reactions. Stopped-flow spectroscopic techniques can provide insight into the reactivity patterns of model {2Fe2S} sub-sites towards protons, and this information contributes to understanding the nature of the biological systems. In this study we have focussed on the influence of the nature of the bridging dithiolate ligand in influencing the kinetics and activation energy parameters for protonation in synthetic sub-sites including Fe2{µ-[S(CH2)nS]}(CO)4(PMe3)2 [n = 2, ethane-1,2-dithiolate (edt) or n = 3, propane-1,3-dithiolate (pdt)], Fe2[(µ-SCH2)2NH](CO)4(PMe3)2 and (NEt4)2{Fe2[(µ-SCH2)2NH](CO)4(CN)2}. Notably we find that (i) the presence of a nitrogen in the dithiolate bridge does not accelerate metal–metal bond protonation, and that (ii) immobilisation of (NEt4)2[Fe2(µ-pdt)(CO)4(CN)2] in a polymer matrix stabilises otherwise short-lifetime protonation products.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Energy Materials Laboratory Faculty of Science > Research Groups > Chemistry of Materials and Catalysis Faculty of Science > Research Groups > Chemistry of Light and Energy Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Synthetic Chemistry (former - to 2017)
Depositing User:	Rachel Smith
Date Deposited:	23 Mar 2011 16:04
Last Modified:	24 Sep 2024 09:07
URI:	https://ueaeprints.uea.ac.uk/id/eprint/27071
DOI:	10.1039/C004692B

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