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FeFe -Hydrogenase active site models with relatively low reduction potentials: Diiron dithiolate complexes containing rigid bridges
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2008 (English)In: Journal of Inorganic Biochemistry, ISSN 0162-0134, E-ISSN 1873-3344, Vol. 102, no 4, 952-959 p.Article in journal (Refereed) Published
Abstract [en]

Three diiron dithiolate complexes containing rigid and conjugated bridges, [mu-SC6H4-2-(CO)S-mu]Fe-2(CO)(6) (1), [2-mu-SC5H3N-3-(CO)S-mu]Fe-2(CO)(6) (2). and the PPh3-monosubstituted complex [mu-SC6H4-2-(CO)S-mu]Fe-2(CO)(5)(PPh3) (1-P), were prepared as biomimetic models for the [FeFe]-hydrogenase active site. The structures of complexes 1 and 2 were determined by single crystal X-ray analysis, which shows that each complex features a rigid coplanar dithiolate bridge with a 2-3 degrees deviation from the bisect plane of the molecule. The influence of the rigid bridge on the reduction potentials of complexes 1, 2 and 1-P was investigated by electrochemistry. The cyclic voltammograms of complexes 1 and 2 display large positive shifts for the primary reduction potentials, that is, 380-480 mV in comparison to that of the pdt-bridged (pdt = propane-1,3-dithiolato) complex (mu-pdt)Fe-2(CO)(6) and 160-260 mV to that of the bdt-bridged (bdt = benzene- 1,2-dithiolato) analogue ([mu-bdt)Fe-2(CO)(6).

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2008. Vol. 102, no 4, 952-959 p.
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URN: urn:nbn:se:kth:diva-17464DOI: 10.1016/j.jinorgbio.2007.12.018ISI: 000255131500038Scopus ID: 2-s2.0-40649110473OAI: oai:DiVA.org:kth-17464DiVA: diva2:335508
Note
QC 20100525Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2017-12-12Bibliographically approved

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Sun, Licheng

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