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Carbene-pyridine chelating 2Fe2S hydrogenase model complexes as highly active catalysts for the electrochemical reduction of protons from weak acid (HOAc)
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2007 (English)In: Dalton Transactions, ISSN 1477-9226, E-ISSN 1477-9234, no 13, p. 1277-1283Article in journal (Refereed) Published
Abstract [en]

Two asymmetrically disubstituted diiron complexes (mu-pdt)[Fe(CO)(3)][Fe(CO)(eta(2)-L)] (L = 1-methyl-3-(2-pyridyl)imidazol-2-ylidene (NHCMePy), 2; 1,3-bis(2-picolyl) imidazol-2-ylidene (NHCdiPic), 4) and a mono-substituted diiron complex (mu-pdt)[Fe(CO)(3)][Fe(CO)(2)(NHCdiPic)] (3) were prepared as biomimetic models of the Fe-only hydrogenase active site. X-Ray studies show that the NHCMePy and NHCdiPic ligands in 2 and 4 each coordinate to the single iron atom as NHC-Py chelating ligands in two basal positions and the NHCdiPic ligand of complex 3 lies in an apical position as a monodentate ligand. The large ranges of the highest and the lowest nu(CO) frequencies of 2 and 4 reflect that the relatively uneven electron density on the two iron atoms of the 2Fe2S model complexes 2 and 4 is as that observed for mono-substituted diiron complexes of good donor ligands. The cyclic voltammograms and the electrochemical proton reduction by 2 and 3 were studied in the presence of HOAc to evaluate the effect of asymmetrical substitution of strong donor ligands on the redox properties of the iron atoms and on the electrocatalytic activity for proton reduction.

Place, publisher, year, edition, pages
2007. no 13, p. 1277-1283
Keywords [en]
fe-only hydrogenases, iron hydrogenase, desulfovibrio-desulfuricans, site models, evolution, ligands, coordination, tertiary, analogs
Identifiers
URN: urn:nbn:se:kth:diva-16463DOI: 10.1039/b616645hISI: 000245030800003PubMedID: 17372642Scopus ID: 2-s2.0-33947376978OAI: oai:DiVA.org:kth-16463DiVA, id: diva2:334505
Note
QC 20100525Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2022-06-25Bibliographically approved

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Sun, Licheng

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