The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre

Johannes Fritsch, Patrick Scheerer (), Stefan Frielingsdorf, Sebastian Kroschinsky, Bärbel Friedrich, Oliver Lenz () and Christian M. T. Spahn ()
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Johannes Fritsch: Mikrobiologie, Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestraße 117
Patrick Scheerer: Institut für Medizinische Physik und Biophysik (CC2), Charité–Universitätsmedizin Berlin, Charitéplatz 1
Stefan Frielingsdorf: Mikrobiologie, Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestraße 117
Sebastian Kroschinsky: Institut für Medizinische Physik und Biophysik (CC2), Charité–Universitätsmedizin Berlin, Charitéplatz 1
Bärbel Friedrich: Mikrobiologie, Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestraße 117
Oliver Lenz: Mikrobiologie, Institut für Biologie, Humboldt-Universität zu Berlin, Chausseestraße 117
Christian M. T. Spahn: Institut für Medizinische Physik und Biophysik (CC2), Charité–Universitätsmedizin Berlin, Charitéplatz 1

Nature, 2011, vol. 479, issue 7372, 249-252

Abstract: Oxygen-tolerant hydrogenases Hydrogenases are metalloprotein enzymes that catalyse the reversible oxidation of dihydrogen to protons and electrons, a critical pathway in anaerobic metabolism. This reaction is of particular interest for hydrogen-based applications, in fuel cells for instance, but many applications are hindered by the high oxygen sensitivity that is an intrinsic feature of most hydrogenases. Two groups report the structures of oxygen-tolerant hydrogenases, one from the soil bacterium Ralstonia eutropha and the other from the marine bacterium Hydrogenovibrio marinus. The structures shed light on how redox-sensitive active-site intermediates are protected from destruction. Both enzymes feature a novel iron-sulphur centre at the active site, coordinated by a group of cysteine residues.

Date: 2011
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DOI: 10.1038/nature10505

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