We thank Drs David Rinaldo and Anne Volbeda for helpful discussions. We appreciate the help from the staff of the computing facility provided by the Commissariat à l’Energie Atomique (CEA/DSV/GIPSI), Saclay, and CCRT, Bruyères-le-Châtel, and thank the CEA and CNRS for institutional funding.
The Structural Plasticity of the Proximal [4Fe3S] Cluster is Responsible for the O2 Tolerance of Membrane-Bound [NiFe] Hydrogenases†
Article first published online: 7 JAN 2013
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 52, Issue 7, pages 2002–2006, February 11, 2013
How to Cite
Mouesca, J.-M., Fontecilla-Camps, J. C. and Amara, P. (2013), The Structural Plasticity of the Proximal [4Fe3S] Cluster is Responsible for the O2 Tolerance of Membrane-Bound [NiFe] Hydrogenases . Angew. Chem. Int. Ed., 52: 2002–2006. doi: 10.1002/anie.201209063
- Issue published online: 6 FEB 2013
- Article first published online: 7 JAN 2013
- Manuscript Received: 12 NOV 2012
- iron–sulfur cluster;
- redox chemistry;
The main difference between O2-sensitive and O2-tolerant [NiFe] hydrogenases is the plasticity of the proximal [4Fe3S] cluster in the latter hydrogenase (see scheme). Deprotonation of a conserved glutamate residue initiates the movement of the iron atom, resulting in its binding to the amide nitrogen atom of one of the two supernumerary cysteine ligands and superoxidation of the proximal cluster.