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
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	2011
卷号	286 期号:24 页码:21287
ISSN号	0021-9258
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.
收录类别	SCI
语种	英语
WOS记录号	WOS:000291464700027
公开日期	2012-07-04
内容类型	期刊论文
源URL	[http://ir.sinap.ac.cn/handle/331007/9470]
专题	上海应用物理研究所_中科院上海应用物理研究所2011-2017年
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]. 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.