Abstract
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.
Original language | English (US) |
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Pages (from-to) | 8842-8855 |
Number of pages | 14 |
Journal | Journal of the American Chemical Society |
Volume | 126 |
Issue number | 28 |
DOIs | |
State | Published - Jul 21 2004 |
All Science Journal Classification (ASJC) codes
- Catalysis
- General Chemistry
- Biochemistry
- Colloid and Surface Chemistry