期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 139, 期 20, 页码 7062-7070出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b02997
关键词
-
资金
- Department of Energy, Office of Science [DE-AC-02-06CH11357]
- National Science Foundation [MCB1404866, CHE-1058931]
- National Institutes of Health [GM40392]
- JSPS KAKENHI [24221005]
- Grants-in-Aid for Scientific Research [16H04172] Funding Source: KAKEN
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据