Raman-Assisted Crystallography Reveals End-On Peroxide Intermediates in a Nonheme Iron Enzyme
- 20 April 2007
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 316 (5823) , 449-453
- https://doi.org/10.1126/science.1138885
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.Keywords
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This publication has 27 references indexed in Scilit:
- Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymesProceedings of the National Academy of Sciences, 2007
- Understanding the Mechanism of Superoxide Reductase Promoted Reduction of SuperoxideEuropean Journal of Inorganic Chemistry, 2006
- Geometries and Electronic Structures of Cyanide Adducts of the Non-Heme Iron Active Site of Superoxide Reductases: Vibrational and ENDOR StudiesBiochemistry, 2005
- Advances in kinetic protein crystallographyPublished by Elsevier ,2005
- Structure and Chemistry of Cytochrome P450Chemical Reviews, 2005
- Spin‐State Rationale for the Peroxo‐Stabilizing Role of the Thiolate Ligand in Superoxide ReductaseAngewandte Chemie International Edition in English, 2005
- Following Ligand Binding and Ligand Reactions in Proteins via Raman CrystallographyBiochemistry, 2004
- The catalytic pathway of horseradish peroxidase at high resolutionNature, 2002
- The Catalytic Pathway of Cytochrome P450cam at Atomic ResolutionScience, 2000
- Reversible Dioxygen Binding to Hemerythrin. 1. Electronic Structures of Deoxy- and OxyhemerythrinJournal of the American Chemical Society, 1999