Nuclear Resonance Vibrational Spectroscopic Definition of Peroxy Intermediates in Nonheme Iron Sites

Kyle D. Sutherlin, Lei V. Liu, Yong Min Lee, Yeonju Kwak, Yoshitaka Yoda, Makina Saito, Masayuki Kurokuzu, Yasuhiro Kobayashi, Makoto Seto, Lawrence Que, Wonwoo Nam, Edward I. Solomon

研究成果: Article査読

4 被引用数 (Scopus)

抄録

FeIII-(hydro)peroxy intermediates have been isolated in two classes of mononuclear nonheme Fe enzymes that are important in bioremediation: the Rieske dioxygenases and the extradiol dioxygenases. The binding mode and protonation state of the peroxide moieties in these intermediates are not well-defined, due to a lack of vibrational structural data. Nuclear resonance vibrational spectroscopy (NRVS) is an important technique for obtaining vibrational information on these and other intermediates, as it is sensitive to all normal modes with Fe displacement. Here, we present the NRVS spectra of side-on FeIII-peroxy and end-on FeIII-hydroperoxy model complexes and assign these spectra using calibrated DFT calculations. We then use DFT calculations to define and understand the changes in the NRVS spectra that arise from protonation and from opening the Fe-O-O angle. This study identifies four spectroscopic handles that will enable definition of the binding mode and protonation state of FeIII-peroxy intermediates in mononuclear nonheme Fe enzymes. These structural differences are important in determining the frontier molecular orbitals available for reactivity.

本文言語English
ページ(範囲)14294-14302
ページ数9
ジャーナルJournal of the American Chemical Society
138
43
DOI
出版ステータスPublished - 2016 11 2
外部発表はい

ASJC Scopus subject areas

  • 触媒
  • 化学 (全般)
  • 生化学
  • コロイド化学および表面化学

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