Biomimetic assembly and activation of [FeFe]-hydrogenases

G. Berggren, A. Adamska, C. Lambertz, T. R. Simmons, J. Esselborn, M. Atta, S. Gambarelli, J.-M. Mouesca, E. Reijerse, W. Lubitz, T. Happe, V. Artero and M. Fontecave ()
Additional contact information
G. Berggren: Laboratoire de Chimie et Biologie des Métaux (CEA/Université Grenoble 1/CNRS), 17 rue des Martyrs, F-38054 Grenoble Cedex 9, France
A. Adamska: Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34–36, 45470 Mülheim an der Ruhr, Germany
C. Lambertz: Lehrstuhl Biochemie der Pflanzen, AG Photobiotechnologie, Ruhr Universität Bochum, Universitätsstrasse 150, 44801 Bochum, Germany
T. R. Simmons: Laboratoire de Chimie et Biologie des Métaux (CEA/Université Grenoble 1/CNRS), 17 rue des Martyrs, F-38054 Grenoble Cedex 9, France
J. Esselborn: Lehrstuhl Biochemie der Pflanzen, AG Photobiotechnologie, Ruhr Universität Bochum, Universitätsstrasse 150, 44801 Bochum, Germany
M. Atta: Laboratoire de Chimie et Biologie des Métaux (CEA/Université Grenoble 1/CNRS), 17 rue des Martyrs, F-38054 Grenoble Cedex 9, France
S. Gambarelli: Laboratoire de Chimie Inorganique et Biologique, (CEA-INAC, Université Grenoble 1, UMR-E 3), 17 rue des Martyrs, F-38054 Grenoble Cedex 9, France
J.-M. Mouesca: Laboratoire de Chimie Inorganique et Biologique, (CEA-INAC, Université Grenoble 1, UMR-E 3), 17 rue des Martyrs, F-38054 Grenoble Cedex 9, France
E. Reijerse: Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34–36, 45470 Mülheim an der Ruhr, Germany
W. Lubitz: Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34–36, 45470 Mülheim an der Ruhr, Germany
T. Happe: Lehrstuhl Biochemie der Pflanzen, AG Photobiotechnologie, Ruhr Universität Bochum, Universitätsstrasse 150, 44801 Bochum, Germany
V. Artero: Laboratoire de Chimie et Biologie des Métaux (CEA/Université Grenoble 1/CNRS), 17 rue des Martyrs, F-38054 Grenoble Cedex 9, France
M. Fontecave: Laboratoire de Chimie et Biologie des Métaux (CEA/Université Grenoble 1/CNRS), 17 rue des Martyrs, F-38054 Grenoble Cedex 9, France

Nature, 2013, vol. 499, issue 7456, 66-69

Abstract: Three synthetic mimics of the di-iron centre in [FeFe]-hydrogenases are loaded onto the HydF protein and then transferred to apo-HydA1; full activation of HydA1 was achieved only with the HydF hybrid protein that contained the mimic with an azadithiolate bridge, confirming the presence of this ligand in the active site of native [FeFe]-hydrogenases.

Date: 2013
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DOI: 10.1038/nature12239

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