Katona Gergely, Carpentier Philippe, Nivière Vincent, Amara Patricia, Adam Virgile, Ohana Jérémy, Tsanov Nikolay, Bourgeois Dominique
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.
Science. 2007 Apr 20;316(5823):449-53. doi: 10.1126/science.1138885.
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.
铁-过氧化物中间体在许多含铁生物分子的反应循环中起着核心作用。我们在超氧化物还原酶（SOR）晶体中捕获了铁（III）-（氢）过氧物种，SOR是一种清除超氧自由基的非血红素单核铁酶。1.95埃分辨率的X射线衍射数据和晶体中记录的拉曼光谱显示，铁-（氢）过氧中间体的（氢）过氧基团以端基方式结合。动态的SOR活性位点促进了瞬态氢键网络的形成，这可能有助于铁-氧键的断裂，从而释放反应产物过氧化氢。
