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Chem Commun (Camb). 2016 Dec 22;53(2):344-347. doi: 10.1039/c6cc08869d.

Reactivity of the nitrogen-centered tryptophanyl radical in the catalysis by the radical SAM enzyme NosL.

Author information

1
College 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.
2
Department of Chemistry, Fudan University, Shanghai, 200433, China. qizhang@sioc.ac.cn.
3
College of Life Science, Fujian Agriculture and Forestry University, Fuzhou, 350002, China. jgaotao@gmail.com.
4
Department of Chemistry, Fudan University, Shanghai, 200433, China. qizhang@sioc.ac.cn and School of Life Sciences, Lanzhou University, Lanzhou, 730000, China.

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.

PMID:
27929146
DOI:
10.1039/c6cc08869d
[Indexed for MEDLINE]

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