Resin-bound models of the [FeFe]-hydrogenase enzyme active site and studies of their reactivity

Kayla N. Green; Jennifer L. Hess; Christine M. Thomas; Marcetta Y. Darensbourg

doi:10.1039/B823152D

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Dalton Transactions

Issue 22, 2009

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Resin-bound models of the [FeFe]-hydrogenase enzyme active site and studies of their reactivity

Kayla N. Green , Jennifer L. Hess , Christine M. Thomas and Marcetta Y. Darensbourg

Dalton Trans., 2009, 4344-4350

DOI: 10.1039/B823152D
Received 24 Dec 2008, Accepted 10 Feb 2009
First published on the web 02 Mar 2009
This article is part of the collection: Bioorganometallic chemistry

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Abstract
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The immobilization of synthetic analogues of the [FeFe]-hydrogenase, [FeFe]H₂ase, enzyme active site on polyethyleneglycol-rich polystyrene beads is described. Using the reactivity of the amine termini of the PEG chains with carboxylates incorporated into (μ-SRS)[Fe(CO)₃]₂ or (μ-SR)₂[Fe(CO)₃]₂ derivative, ν(CO)IR signatures can be used to interrogate the structure and properties of the diiron carbonyl complexes once incorporated into the PEG environment of the polymer beads. Alternatively, the SRS dithiolate was first attached to the resin and the diiron unit assembled via an in situ process on the bead.

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Resin-bound models of the [FeFe]-hydrogenase enzyme active site and studies of their reactivity

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