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Extending the motif of the [FeFe]-hydrogenase active site models: Protonation of Fe2(NR)2(CO)6−x L x species
- Source :
-
Journal of Inorganic Biochemistry . Nov2007, Vol. 101 Issue 11/12, p1748-1751. 4p. - Publication Year :
- 2007
-
Abstract
- Abstract: Studies on diiron dithiolato complexes have proven fruitful for modeling the active site of the [FeFe]-hydrogenases. Here we present a departure from the classical Fe2S2 motif by examining the viability of Fe2N2 butterfly compounds as functional models for the diiron active site of [FeFe]-hydrogenases. Derivatization of Fe2(BC)(CO)6 (1, BC=benzo-[c]-cinnoline) with PMe3 affords Fe2(BC)(CO)4(PMe3)2, which subsequently undergoes protonation at the Fe–Fe bond. The hydride [(μ-H)Fe2(BC)(CO)4(PMe3)2]PF6 was characterized crystallographically as the C 2v isomer. It represents a rare example of a hydrido diiron complex that exists as observable isomers, depending on the location of the phosphine ligands – diapical and apical–basal. This hydride catalyzes the electrochemical reduction of protons. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 01620134
- Volume :
- 101
- Issue :
- 11/12
- Database :
- Academic Search Index
- Journal :
- Journal of Inorganic Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 27152393
- Full Text :
- https://doi.org/10.1016/j.jinorgbio.2007.05.005