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.
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DOI：
10.1016/j.jinorgbio.2007.05.005
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发表时间：
2007-11
影响因子：
3.9
通讯作者：
Phillip I. Volkers;T. Rauchfuss
中科院分区：
文献类型：
--
作者：
Phillip I. Volkers;T. Rauchfuss
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 Fe2S2motif by examining the viability of Fe2N2butterfly compounds as functional models for the diiron active site of [FeFe]-hydrogenases. Derivatization of Fe2(BC)(CO)6(1, BC=benzo-[c]-cinnoline) with PMe3affords 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]PF6was characterized crystallographically as the C2visomer. 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.
