Peroxide Activation for Electrophilic Reactivity by the Binuclear Non-heme Iron Enzyme AurF

Kiyoung Park, Ning Li, Yeonju Kwak, Martin Srnec, Caleb B. Bell, Lei V. Liu, Shaun D. Wong, Yoshitaka Yoda, Shinji Kitao, Makoto Seto, Michael Hu, Jiyong Zhao, Carsten Krebs, J. Martin Bollinger, Edward I. Solomon

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45 Scopus citations


Binuclear non-heme iron enzymes activate O2 for diverse chemistries that include oxygenation of organic substrates and hydrogen atom abstraction. This process often involves the formation of peroxo-bridged biferric intermediates, only some of which can perform electrophilic reactions. To elucidate the geometric and electronic structural requirements to activate peroxo reactivity, the active peroxo intermediate in 4-aminobenzoate N-oxygenase (AurF) has been characterized spectroscopically and computationally. A magnetic circular dichroism study of reduced AurF shows that its electronic and geometric structures are poised to react rapidly with O2. Nuclear resonance vibrational spectroscopic definition of the peroxo intermediate formed in this reaction shows that the active intermediate has a protonated peroxo bridge. Density functional theory computations on the structure established here show that the protonation activates peroxide for electrophilic/single-electron-transfer reactivity. This activation of peroxide by protonation is likely also relevant to the reactive peroxo intermediates in other binuclear non-heme iron enzymes.

Original languageEnglish (US)
Pages (from-to)7062-7070
Number of pages9
JournalJournal of the American Chemical Society
Issue number20
StatePublished - May 24 2017

All Science Journal Classification (ASJC) codes

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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