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

Haocheng Qianzhu, Wenjuan Ji, Xinjian Ji, Leixia Chu, Chuchu Guo, Wei Lu, Wei Ding, Jiangtao Gao*, Qi Zhang

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)344-347
Number of pages4
JournalChemical Communications
Volume53
Issue number2
DOIs
Publication statusPublished - 2017
Externally publishedYes

Fingerprint

Dive into the research topics of 'Reactivity of the nitrogen-centered tryptophanyl radical in the catalysis by the radical SAM enzyme NosL'. Together they form a unique fingerprint.

Cite this