Journal of the American Chemical Society, 2004-07, Vol.126 (28), p.8842-8855
2004
Volltextzugriff (PDF)
Details
- Autor(en) / Beteiligte
- Titel
- Nature of the Peroxo Intermediate of the W48F/D84E Ribonucleotide Reductase Variant: Implications for O2 Activation by Binuclear Non-Heme Iron Enzymes
- Ist Teil von
- Journal of the American Chemical Society, 2004-07, Vol.126 (28), p.8842-8855
- Ort / Verlag
- Washington, DC: American Chemical Society
- Erscheinungsjahr
- 2004
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- Analysis of the spectroscopic signatures of the R2-W48F/D84E biferric peroxo intermediate identifies a cis μ-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 μ-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 μ-1,2 peroxo model complexes, and other enzymatic biferric peroxo intermediates.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0002-7863eISSN: 1520-5126DOI: 10.1021/ja049106aTitel-ID: cdi_pubmed_primary_15250738
- Format
- –
- Schlagworte
- Binding Sites - genetics, Binding Sites - physiology, Biological and medical sciences, Computer Simulation, Electronic structure, Ferrous Compounds - chemistry, Fundamental and applied biological sciences. Psychology, Models, Chemical, Models, Molecular, Molecular biophysics, Mutagenesis, Site-Directed, Nonheme Iron Proteins - chemistry, Oxygen - chemistry, Peroxides - chemistry, Ribonucleotide Reductases - analysis, Ribonucleotide Reductases - chemistry, Spectrum Analysis, Raman - methods, Structure in molecular biology