Mechanistic aspects of the protonation of [FeFe]-hydrogenase subsite analogues

Aušra Jablonskytė; Joseph A Wright; Christopher J Pickett

doi:10.1039/B923191A

Mechanistic aspects of the protonation of [FeFe]-hydrogenase subsite analogues

Aušra Jablonskytė
, Joseph A Wright
, Christopher J Pickett

Synthetic and Medicinal Chemistry

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

62 Citations (Scopus)

Abstract

The formation of transient metal hydride(s) at the metallo-sulfur active sites of [FeFe]-hydrogenase is implicated in both hydrogen evolution and uptake reactions. Using a combination of time-resolved NMR, stopped-flow UV and stopped-flow IR, we have begun to unravel the mechanisms for protonation of synthetic electron-rich analogues of the di-iron subsite of the enzyme: Fe₂(µ-pdt)(CO)₄(PMe₃)₂, Fe₂(µ-edt)(CO)₄(PMe₃)₂, (NEt₄)₂[Fe₂(µ-pdt)(CO)₄(CN)₂], (NEt₄)₂[Fe₂(µ-edt)(CO)₄(PMe₃)₂] and (NEt₄)[Fe₂(µ-pdt)(CO)₄(CN)(PMe₃)] (pdt = propane-1,3-dithiolate, edt = ethane-1,2-dithiolate). The mechanistic role of isomer interconversion and how this critically relates to steric access to the di-iron bridge are revealed.)] (pdt = propane-1,3-dithiolate, edt = ethane-1,2-dithiolate). The mechanistic role of isomer interconversion and how this critically relates to steric access to the di-iron bridge are revealed.

Original language	English
Pages (from-to)	3026-3034
Number of pages	9
Journal	Dalton Transactions
Volume	39
Issue number	12
DOIs	https://doi.org/10.1039/B923191A
Publication status	Published - 2010

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10.1039/B923191A

Cite this

@article{e43bb71aea174c0c9dedcfe5922f529c,

title = "Mechanistic aspects of the protonation of [FeFe]-hydrogenase subsite analogues",

abstract = "The formation of transient metal hydride(s) at the metallo-sulfur active sites of [FeFe]-hydrogenase is implicated in both hydrogen evolution and uptake reactions. Using a combination of time-resolved NMR, stopped-flow UV and stopped-flow IR, we have begun to unravel the mechanisms for protonation of synthetic electron-rich analogues of the di-iron subsite of the enzyme: Fe2(µ-pdt)(CO)4(PMe3)2, Fe2(µ-edt)(CO)4(PMe3)2, (NEt4)2[Fe2(µ-pdt)(CO)4(CN)2], (NEt4)2[Fe2(µ-edt)(CO)4(PMe3)2] and (NEt4)[Fe2(µ-pdt)(CO)4(CN)(PMe3)] (pdt = propane-1,3-dithiolate, edt = ethane-1,2-dithiolate). The mechanistic role of isomer interconversion and how this critically relates to steric access to the di-iron bridge are revealed.)] (pdt = propane-1,3-dithiolate, edt = ethane-1,2-dithiolate). The mechanistic role of isomer interconversion and how this critically relates to steric access to the di-iron bridge are revealed.",

author = "Au{\v s}ra Jablonskytė and Wright, \{Joseph A\} and Pickett, \{Christopher J\}",

year = "2010",

doi = "10.1039/B923191A",

language = "English",

volume = "39",

pages = "3026--3034",

journal = "Dalton Transactions",

issn = "1477-9234",

publisher = "Royal Society of Chemistry",

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TY - JOUR

T1 - Mechanistic aspects of the protonation of [FeFe]-hydrogenase subsite analogues

AU - Jablonskytė, Aušra

AU - Wright, Joseph A

AU - Pickett, Christopher J

PY - 2010

Y1 - 2010

N2 - The formation of transient metal hydride(s) at the metallo-sulfur active sites of [FeFe]-hydrogenase is implicated in both hydrogen evolution and uptake reactions. Using a combination of time-resolved NMR, stopped-flow UV and stopped-flow IR, we have begun to unravel the mechanisms for protonation of synthetic electron-rich analogues of the di-iron subsite of the enzyme: Fe2(µ-pdt)(CO)4(PMe3)2, Fe2(µ-edt)(CO)4(PMe3)2, (NEt4)2[Fe2(µ-pdt)(CO)4(CN)2], (NEt4)2[Fe2(µ-edt)(CO)4(PMe3)2] and (NEt4)[Fe2(µ-pdt)(CO)4(CN)(PMe3)] (pdt = propane-1,3-dithiolate, edt = ethane-1,2-dithiolate). The mechanistic role of isomer interconversion and how this critically relates to steric access to the di-iron bridge are revealed.)] (pdt = propane-1,3-dithiolate, edt = ethane-1,2-dithiolate). The mechanistic role of isomer interconversion and how this critically relates to steric access to the di-iron bridge are revealed.

AB - The formation of transient metal hydride(s) at the metallo-sulfur active sites of [FeFe]-hydrogenase is implicated in both hydrogen evolution and uptake reactions. Using a combination of time-resolved NMR, stopped-flow UV and stopped-flow IR, we have begun to unravel the mechanisms for protonation of synthetic electron-rich analogues of the di-iron subsite of the enzyme: Fe2(µ-pdt)(CO)4(PMe3)2, Fe2(µ-edt)(CO)4(PMe3)2, (NEt4)2[Fe2(µ-pdt)(CO)4(CN)2], (NEt4)2[Fe2(µ-edt)(CO)4(PMe3)2] and (NEt4)[Fe2(µ-pdt)(CO)4(CN)(PMe3)] (pdt = propane-1,3-dithiolate, edt = ethane-1,2-dithiolate). The mechanistic role of isomer interconversion and how this critically relates to steric access to the di-iron bridge are revealed.)] (pdt = propane-1,3-dithiolate, edt = ethane-1,2-dithiolate). The mechanistic role of isomer interconversion and how this critically relates to steric access to the di-iron bridge are revealed.

U2 - 10.1039/B923191A

DO - 10.1039/B923191A

M3 - Article

SN - 1477-9234

VL - 39

SP - 3026

EP - 3034

JO - Dalton Transactions

JF - Dalton Transactions

IS - 12

ER -