Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 126, Issue 28, Pages 8842-8855Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja049106a
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- NIGMS NIH HHS [GM55365] Funding Source: Medline
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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.
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