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学科主题: 生命有机化学
题名: Characterization of NocL Involved in Thiopeptide Nocathiacin I Biosynthesis A [4Fe-4S] CLUSTER AND THE CATALYSIS OF A RADICAL S-ADENOSYLMETHIONINE ENZYME
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
作者: ZHANG QI ; CHEN DANDAN ; LIN JUN ; LIAO RIJING ; TONG WEI ; XU ZHINAN ; Liu W(刘文)
通讯作者: 刘文
刊名: J. Biol. Chem.
发表日期: 2011
卷: 286, 期:24, 页:21287-21294
收录类别: SCI
部门归属: 中科院上海有机化学研究所; 浙江大学; 中科院上海应用物理研究所; 中科院合肥物质科学研究院
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.
语种: 英语
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WOS记录号: WOS:000291464700027
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/28473
Appears in Collections:生命有机化学国家重点实验室_期刊论文

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Recommended Citation:
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.
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