Mechanistic aspects of the protonation of [FeFe]-hydrogenase subsite analogues

Jablonskytė, Aušra, Wright, Joseph A ORCID: https://orcid.org/0000-0001-9603-1001 and Pickett, Christopher J (2010) Mechanistic aspects of the protonation of [FeFe]-hydrogenase subsite analogues. Dalton Transactions, 39 (12). pp. 3026-3034. ISSN 1477-9234

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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. Using a combination of time-resolved NMR, stopped-flow UV and stopped-flow IR, we have begun to unravel the mechanisms for protonation of synthetic electron-rich analogues of the di-iron subsite of the enzyme: Fe2(µ-pdt)(CO)4(PMe3)2, Fe2(µ-edt)(CO)4(PMe3)2, (NEt4)2[Fe2(µ-pdt)(CO)4(CN)2], (NEt4)2[Fe2(µ-edt)(CO)4(PMe3)2] and (NEt4)[Fe2(µ-pdt)(CO)4(CN)(PMe3)] (pdt = propane-1,3-dithiolate, edt = ethane-1,2-dithiolate). The mechanistic role of isomer interconversion and how this critically relates to steric access to the di-iron bridge are revealed.)] (pdt = propane-1,3-dithiolate, edt = ethane-1,2-dithiolate). The mechanistic role of isomer interconversion and how this critically relates to steric access to the di-iron bridge are revealed.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Chemistry
UEA Research Groups:	Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Synthetic Chemistry (former - to 2017) 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 > Energy Materials Laboratory
Depositing User:	Rachel Smith
Date Deposited:	23 Mar 2011 15:58
Last Modified:	04 Jan 2023 13:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/27073
DOI:	10.1039/B923191A

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