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 ; LIAO RIJING ; TONG WEI ; XU ZHINAN ; Liu W(刘文)
刊名	J. Biol. Chem.
	2011
卷号	286 期号:24 页码:21287-21294
ISSN号	0021-9258
其他题名	Characterization of NocL Involved in Thiopeptide Nocathiacin I Biosynthesis A [4Fe-4S] CLUSTER AND THE CATALYSIS OF A RADICAL S-ADENOSYLMETHIONINE ENZYME
通讯作者	刘文
英文摘要	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.
学科主题	生命有机化学
收录类别	SCI
原文出处	http://dx.doi.org/10.1074/jbc.M111.224832
语种	英语
WOS记录号	WOS:000291464700027
公开日期	2013-08-23
内容类型	期刊论文
源URL	[http://202.127.28.38/handle/331003/28473]
专题	上海有机化学研究所_生命有机化学国家重点实验室
推荐引用方式 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]. J. Biol. Chem.,2011,286(24):21287-21294.
APA	ZHANG QI.,CHEN DANDAN.,LIN JUN.,LIAO RIJING.,TONG WEI.,...&刘文.(2011).Characterization of NocL Involved in Thiopeptide Nocathiacin I Biosynthesis A [4Fe-4S] CLUSTER AND THE CATALYSIS OF A RADICAL S-ADENOSYLMETHIONINE ENZYME.J. Biol. Chem.,286(24),21287-21294.
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".J. Biol. Chem. 286.24(2011):21287-21294.