کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1317080 | 1499481 | 2007 | 4 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Extending the motif of the [FeFe]-hydrogenase active site models: Protonation of Fe2(NR)2(CO)6−xLx species Extending the motif of the [FeFe]-hydrogenase active site models: Protonation of Fe2(NR)2(CO)6−xLx species](/preview/png/1317080.png)
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 C2v 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.
Journal: Journal of Inorganic Biochemistry - Volume 101, Issues 11–12, November 2007, Pages 1748–1751