Nature of the peroxo intermediate of the W48F/D84E ribonucleotide reductase variant

Implications for O2 activation by binuclear non-heme iron enzymes

Andrew J. Skulan, Thomas C. Brunold, Jeffrey Baldwin, Lana Saleh, Joseph M. Bollinger, Jr., Edward I. Solomon

Research output: Contribution to journalArticle

69 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)8842-8855
Number of pages14
JournalJournal of the American Chemical Society
Volume126
Issue number28
DOIs
StatePublished - Jul 21 2004

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Ribonucleotide Reductases
Iron
Enzymes
Chemical activation
Geometry
Proteins
Discrete Fourier transforms
Electronic structure
Oxidoreductases

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

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Nature of the peroxo intermediate of the W48F/D84E ribonucleotide reductase variant : Implications for O2 activation by binuclear non-heme iron enzymes. / Skulan, Andrew J.; Brunold, Thomas C.; Baldwin, Jeffrey; Saleh, Lana; Bollinger, Jr., Joseph M.; Solomon, Edward I.

In: Journal of the American Chemical Society, Vol. 126, No. 28, 21.07.2004, p. 8842-8855.

Research output: Contribution to journalArticle

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