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Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic

Nature Chemical Biology volume 9, pages 607–609 (2013)Cite this article

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Abstract

Hydrogenases catalyze the formation of hydrogen. The cofactor ('H-cluster') of [FeFe]-hydrogenases consists of a [4Fe-4S] cluster bridged to a unique [2Fe] subcluster whose biosynthesis in vivo requires hydrogenase-specific maturases. Here we show that a chemical mimic of the [2Fe] subcluster can reconstitute apo-hydrogenase to full activity, independent of helper proteins. The assembled H-cluster is virtually indistinguishable from the native cofactor. This procedure will be a powerful tool for developing new artificial H2-producing catalysts.

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Figure 1: The H-cluster is assembled from a regular [4Fe-4S] cluster and a unique [2Fe] subcluster.
Figure 2: Various types of HYDA enzymes can be spontaneously activated by [2Fe]MIM and behave like the natural enzymes.
Figure 3: The chemically reconstituted H-cluster is virtually indistinguishable from the native form.

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Acknowledgements

This work was supported by the Bundesministerium für Bildung und Forschung Bio-H2 project (to T.H. and W.L.), the Max Planck Society, the French National Research Agency (NiFe–Cat ANR–10–BLAN–711 and Labex Program ARCANE 11–LABX–003 to T.S.,V.A. and M.F.) and the European Research Council under the European Union's Seventh Framework Programme (FP/2007-2013/ERC grant agreement no. 306398 to V.A.). G.B. gratefully acknowledges the Bengt Lundqvist Minnesfond, The Swedish Research Council for Environment, Agricultural Sciences and Spatial Planning (contract no. 213-2010-563) and the Swedish Royal Academy of Sciences. T.H. gratefully acknowledges support from the Deutsche Forschungsgemeinschaft (HA 255/2-1) and the Volkswagen foundation (LigH2t). J.E. is financed by the Studienstiftung des deutschen Volkes.

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Author notes

  1. Gustav Berggren

    Present address: Present address: Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.,

  2. Camilla Lambertz, Agnieszka Adamska-Venkatesh and Trevor Simmons: These authors contributed equally to this work.

Authors and Affiliations

  1. Ruhr-Universität Bochum, Fakultät für Biologie und Biotechnologie, AG Photobiotechnologie, Bochum, Germany

    Julian Esselborn, Camilla Lambertz, Jens Noth, Anja Hemschemeier & Thomas Happe

  2. Max-Planck-Institut für Chemische Energiekonversion, Mülheim an der Ruhr, Germany

    Agnieszka Adamska-Venkatesh, Judith Siebel, Edward Reijerse & Wolfgang Lubitz

  3. Laboratoire de Chimie et Biologie des Métaux (Commissariat à l'énergie atomique et aux énergies alternatives–Université Grenoble 1–Centre national de la recherche scientifique), Grenoble, France

    Trevor Simmons, Gustav Berggren, Vincent Artero & Marc Fontecave

  4. Collège de France, Paris, France

    Marc Fontecave

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Contributions

C.L., J.E., J.N., A.H., M.F., W.L. and T.H. conceived and designed experiments. C.L., J.S., J.E., J.N. and A.A. performed the experiments. C.L., J.E., J.N., A.H., A.A. and T.H. analyzed the data. G.B., T.S., V.A. and M.F. provided the [2Fe]MIM and [2Fe]pdt complexes. A.A., E.R. and W.L. performed and analyzed the EPR and FTIR experiments. All of the authors discussed the results. A.H., J.E. and T.H. wrote the manuscript.

Corresponding author

Correspondence to Thomas Happe.

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The authors declare no competing financial interests.

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Supplementary Results and Supplementary Figures 1–3. (PDF 792 kb)

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Esselborn, J., Lambertz, C., Adamska-Venkatesh, A. et al. Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic. Nat Chem Biol 9, 607–609 (2013). https://doi.org/10.1038/nchembio.1311

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