Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme. - Groupe Métalloprotéines / Metalloproteins Group (IBS-METALLO) Access content directly
Journal Articles Science Year : 2007

Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.

Abstract

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.
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Dates and versions

hal-01075775 , version 1 (20-10-2014)

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Gergely Katona, Philippe Carpentier, Vincent Nivière, Patricia Amara, Virgile Adam, et al.. Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.. Science, 2007, pp.449-53. ⟨hal-01075775⟩
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