title: Nature of the peroxo intermediate of the W48F/D84E ribonucleotide reductase variant: implications for O2 activation by binuclear non-heme iron enzymes.
abstract: Analysis of the spectroscopic signatures of the R2-W48F/D84E biferric peroxo intermediate identifies a cis mu-1,2 peroxo coordination geometry. DFT geometry optimizations on both R2-W48F/D84E and R2-wild-type peroxo intermediate models including constraints imposed by the protein also identify the cis mu-1,2 peroxo geometry as the most stable peroxo intermediate structure. This study provides significant insight into the electronic structure and reactivity of the R2-W48F/D84E peroxo intermediate, structurally related cis mu-1,2 peroxo model complexes, and other enzymatic biferric peroxo intermediates.
authors.affiliation: Department of Chemistry, Stanford University, Stanford, California 94305, USA.
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Skulan
authors.forename: Thomas C
authors.initials: TC
authors.lastname: Brunold
authors.forename: Jeffrey
authors.initials: J
authors.lastname: Baldwin
authors.forename: Lana
authors.initials: L
authors.lastname: Saleh
authors.forename: J Martin
authors.initials: JM
authors.lastname: Bollinger
authors.forename: Edward I
authors.initials: EI
authors.lastname: Solomon
mesh_terms: D001665:Binding Sites / Q000235:genetics / Q000502:physiology; D003198:Computer Simulation; D005296:Ferrous Compounds / Q000737:chemistry; D008956:Models, Chemical; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D019159:Nonheme Iron Proteins / Q000737:chemistry*; D010100:Oxygen / Q000737:chemistry*; D010545:Peroxides / Q000737:chemistry; D012264:Ribonucleotide Reductases / Q000032:analysis / Q000737:chemistry*; D013059:Spectrum Analysis, Raman / Q000379:methods
chemical_list: D005296:Ferrous Compounds; D019159:Nonheme Iron Proteins; D010545:Peroxides; D012264:Ribonucleotide Reductases; C108427:ribonucleotide reductase R2 subunit; D010100:Oxygen