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Updated: Mar 10, 2026

Detection of Nitric Oxide and Superoxide Radical Anion by Electron Paramagnetic Resonance Spectroscopy from Cells using Spin Traps
Published on: August 18, 2012
Reactivity of the nitrogen-centered tryptophanyl radical in the catalysis by the radical SAM enzyme NosL
Haocheng Qianzhu1, Wenjuan Ji2, Xinjian Ji2
1College of Life Science, Fujian Agriculture and Forestry University, Fuzhou, 350002, China. jgaotao@gmail.com and Department of Chemistry, Fudan University, Shanghai, 200433, China. qizhang@sioc.ac.cn.
Abstract:
The radical SAM tryptophan (Trp) lyase NosL involved in nosiheptide biosynthesis catalyzes two parallel reactions, converting l-Trp to 3-methyl-2-indolic acid (MIA) and to dehydroglycine and 3-methylindole, respectively. The two parallel reactions diverge from a nitrogen-centered tryptophanyl radical intermediate. Here we report an investigation on the intrinsic reactivity of the tryptophanyl radical using a chemical model study and DFT calculations. The kinetics of the formation and fragmentation of this nitrogen-centered radical in NosL catalysis were also studied in detail. Our analysis explains the intriguing catalytic promiscuity of NosL and highlights the remarkable role this enzyme plays in achieving an energetically highly unfavorable transformation.
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