Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.
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.
Katona
Gergely
G
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.
Carpentier
Philippe
P
Nivière
Vincent
V
Amara
Patricia
P
Adam
Virgile
V
Ohana
Jérémy
J
Tsanov
Nikolay
N
Bourgeois
Dominique
D
D003460:Crystallization; D018360:Crystallography, X-Ray; D020564:Deltaproteobacteria / Q000201:enzymology*; D005290:Ferric Compounds / Q000737:chemistry / Q000378:metabolism; D006860:Hydrogen Bonding; D006861:Hydrogen Peroxide / Q000737:chemistry* / Q000378:metabolism; D007501:Iron / Q000737:chemistry*; D008024:Ligands; D008956:Models, Chemical; D008958:Models, Molecular; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D010100:Oxygen / Q000737:chemistry; D010545:Peroxides / Q000737:chemistry*; D011487:Protein Conformation; D011522:Protons; D013059:Spectrum Analysis, Raman
D005290:Ferric Compounds; D008024:Ligands; D010545:Peroxides; D011522:Protons; D006861:Hydrogen Peroxide; D007501:Iron; D010088:Oxidoreductases; C121849:superoxide reductase; D010100:Oxygen