Characterization of NocL Involved in Thiopeptide Nocathiacin I Biosynthesis A [4Fe-4S] CLUSTER AND THE CATALYSIS OF A RADICAL S-ADENOSYLMETHIONINE ENZYME

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	Characterization of NocL Involved in Thiopeptide Nocathiacin I Biosynthesis A [4Fe-4S] CLUSTER AND THE CATALYSIS OF A RADICAL S-ADENOSYLMETHIONINE ENZYME
	Zhang, Qi; Chen, Dandan; Lin, Jun(林俊）; Liao, Rijing; Tong, Wei; Xu, Zhinan; Liu, Wen
	2011
Source Publication	JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN	0021-9258
Volume	286 Issue:24 Pages:21287
Abstract	The radical S-adenosylmethionine (AdoMet) enzyme superfamily is remarkable at catalyzing chemically diverse and complex reactions. We have previously shown that NosL, which is involved in forming the indole side ring of the thiopeptide nosiheptide, is a radical AdoMet enzyme that processes L-Trp to afford 3-methyl-2-indolic acid (MIA) via an unusual fragmentation-recombination mechanism. We now report the expansion of the MIA synthase family by characterization of NocL, which is involved in nocathiacin I biosynthesis. EPR and UV-visible absorbance spectroscopic analyses demonstrated the interaction between L-Trp and the [4Fe-4S] cluster of NocL, leading to the assumption of nonspecific interaction of [4Fe-4S] cluster with other nucleophiles via the unique Fe site. This notion is supported by the finding of the heterogeneity in the [4Fe-4S] cluster of NocL in the absence of AdoMet, which was revealed by the EPR study at very low temperature. Furthermore, a free radical was observed by EPR during the catalysis, which is in good agreement with the hypothesis of a glycyl radical intermediate. Combined with the mutational analysis, these studies provide new insights into the function of the [4Fe-4S] cluster of radical AdoMet enzymes as well as the mechanism of the radical-mediated complex carbon chain rearrangement catalyzed by MIA synthase.
Indexed By	SCI
Language	英语
Funding Project	应物所项目组
WOS ID	WOS:000291464700027
Citation statistics	Cited Times:31[WOS] [WOS Record] [Related Records in WOS]
Document Type	期刊论文
Identifier	http://ir.sinap.ac.cn/handle/331007/9470
Collection	中科院上海应用物理研究所2011-2019年
Recommended Citation GB/T 7714	Zhang, Qi,Chen, Dandan,Lin, Jun,et al. Characterization of NocL Involved in Thiopeptide Nocathiacin I Biosynthesis A [4Fe-4S] CLUSTER AND THE CATALYSIS OF A RADICAL S-ADENOSYLMETHIONINE ENZYME[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2011,286(24):21287.
APA	Zhang, Qi.,Chen, Dandan.,Lin, Jun.,Liao, Rijing.,Tong, Wei.,...&Liu, Wen.(2011).Characterization of NocL Involved in Thiopeptide Nocathiacin I Biosynthesis A [4Fe-4S] CLUSTER AND THE CATALYSIS OF A RADICAL S-ADENOSYLMETHIONINE ENZYME.JOURNAL OF BIOLOGICAL CHEMISTRY,286(24),21287.
MLA	Zhang, Qi,et al."Characterization of NocL Involved in Thiopeptide Nocathiacin I Biosynthesis A [4Fe-4S] CLUSTER AND THE CATALYSIS OF A RADICAL S-ADENOSYLMETHIONINE ENZYME".JOURNAL OF BIOLOGICAL CHEMISTRY 286.24(2011):21287.

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