Extending the motif of the [FeFe]-hydrogenase active site models: protonation of Fe2(NR)2(CO)6-xLx species.

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 Fe(2)S(2) motif by examining the viability of Fe(2)N(2) butterfly compounds as functional models for the diiron active site of [FeFe]-hydrogenases. Derivatization of Fe(2)(BC)(CO)(6) (1, BC=benzo-[c]-cinnoline) with PMe(3) affords Fe(2)(BC)(CO)(4)(PMe(3))(2), which subsequently undergoes protonation at the Fe-Fe bond. The hydride [(mu-H)Fe(2)(BC)(CO)(4)(PMe(3))(2)]PF(6) 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.

SUBMITTER: Volkers PI 

PROVIDER: S-EPMC2440487 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature