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Issue 22, 2009
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Resin-bound models of the [FeFe]-hydrogenase enzyme active site and studies of their reactivity

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Abstract

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.

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

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Publication details

The article was received on 24 Dec 2008, accepted on 10 Feb 2009 and first published on 02 Mar 2009


Article type: Paper
DOI: 10.1039/B823152D
Citation: Dalton Trans., 2009, 4344-4350
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    Resin-bound models of the [FeFe]-hydrogenase enzyme active site and studies of their reactivity

    K. N. Green, J. L. Hess, C. M. Thomas and M. Y. Darensbourg, Dalton Trans., 2009, 4344
    DOI: 10.1039/B823152D

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