2017年5月
Peroxide Activation for Electrophilic Reactivity by the Binuclear Non-heme Iron Enzyme AurF
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- 巻
- 139
- 号
- 20
- 開始ページ
- 7062
- 終了ページ
- 7070
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1021/jacs.7b02997
- 出版者・発行元
- AMER CHEMICAL SOC
Binuclear non-heme iron enzymes activate O-2 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 O-2. 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.
- リンク情報
- ID情報
-
- DOI : 10.1021/jacs.7b02997
- ISSN : 0002-7863
- PubMed ID : 28457126
- Web of Science ID : WOS:000402498500041