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Science 20 April 2007:
Vol. 316. no. 5823, pp. 449 - 453
DOI: 10.1126/science.1138885
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Reports

Raman-Assisted Crystallography Reveals End-On Peroxide Intermediates in a Nonheme Iron Enzyme

Gergely Katona,1 Philippe Carpentier,1 Vincent Nivière,2 Patricia Amara,1 Virgile Adam,3 Jérémy Ohana,1 Nikolay Tsanov,1 Dominique Bourgeois1,3*

Iron-peroxide intermediates are central in the reaction cycle of many iron-containing biomolecules. We trapped iron(III)-(hydro)peroxo species in crystals of superoxide reductase (SOR), a nonheme mononuclear iron enzyme that scavenges superoxide radicals. X-ray diffraction data at 1.95 angstrom resolution and Raman spectra recorded in crystallo revealed iron-(hydro)peroxo intermediates with the (hydro)peroxo group bound end-on. The dynamic SOR active site promotes the formation of transient hydrogen bond networks, which presumably assist the cleavage of the iron-oxygen bond in order to release the reaction product, hydrogen peroxide.

1 Institut de Biologie Structurale (IBS) Jean-Pierre Ebel, Commissariat à l'Energie Atomique (CEA), Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble, France.
2 Laboratoire de Chimie et Biologie des Métaux, Institut de Recherches en Technologies et Sciences pour le Vivant, CEA, CNRS, Université J. Fourier, UMR 5249, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France.
3 European Synchrotron Radiation Facility (ESRF), 6 rue Jules Horowitz, BP 220, 38043 Grenoble Cedex, France.

* To whom correspondence should be addressed. E-mail: dominique.bourgeois{at}ibs.fr

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Science. ISSN 0036-8075 (print), 1095-9203 (online)