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

Phillip I. Volkers; Thomas B. Rauchfuss

doi:10.1016/j.jinorgbio.2007.05.005

Extending the motif of the [FeFe]-hydrogenase active site models: Protonation of Fe₂(NR)₂(CO)_6-xL_x species

Phillip I. Volkers, Thomas B. Rauchfuss

Chemistry

Research output: Contribution to journal › Article › peer-review

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.

Original language	English (US)
Pages (from-to)	1748-1751
Number of pages	4
Journal	Journal of Inorganic Biochemistry
Volume	101
Issue number	11-12
DOIs	https://doi.org/10.1016/j.jinorgbio.2007.05.005
State	Published - Nov 2007

Keywords

Electrocatalysis
Fe complexes
Hydrogenase
Metal hydride

ASJC Scopus subject areas

Biochemistry
Inorganic Chemistry

Online availability

10.1016/j.jinorgbio.2007.05.005

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Cite this

@article{3ed1bc9a96b24b52864550ca138569bb,

title = "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 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.",

keywords = "Electrocatalysis, Fe complexes, Hydrogenase, Metal hydride",

author = "Volkers, {Phillip I.} and Rauchfuss, {Thomas B.}",

note = "Funding Information: This work was supported by the United States National Institutes of Health. ",

year = "2007",

month = nov,

doi = "10.1016/j.jinorgbio.2007.05.005",

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T2 - Protonation of Fe2(NR)2(CO)6-xLx species

AU - Volkers, Phillip I.

AU - Rauchfuss, Thomas B.

N1 - Funding Information: This work was supported by the United States National Institutes of Health.

PY - 2007/11

Y1 - 2007/11

N2 - 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.

AB - 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.

KW - Electrocatalysis

KW - Fe complexes

KW - Hydrogenase

KW - Metal hydride

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