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Issue 52, 2018
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X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster

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Abstract

The crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni–Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O2 sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype.

Graphical abstract: X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster

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Supplementary files

Publication details

The article was received on 11 Apr 2018, accepted on 04 Jun 2018 and first published on 05 Jun 2018


Article type: Communication
DOI: 10.1039/C8CC02896F
Citation: Chem. Commun., 2018,54, 7175-7178

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    X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster

    A. Volbeda, J. M. Mouesca, C. Darnault, M. M. Roessler, A. Parkin, F. A. Armstrong and J. C. Fontecilla-Camps, Chem. Commun., 2018, 54, 7175
    DOI: 10.1039/C8CC02896F

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