Journal
SCIENCE
Volume 316, Issue 5823, Pages 449-453Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1138885
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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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