Investigation of enzymatic C-P bond formation using multiple quantum HCP nuclear magnetic resonance spectroscopy
文献类型：期刊论文
| 作者 | Hu, Kaifeng1,2 ; Werner, Williard J.3; Allen, Kylie D.3,4; Wang, Susan C.3
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| 刊名 | MAGNETIC RESONANCE IN CHEMISTRY
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| 出版日期 | 2015-04-01 |
| 卷号 | 53期号:4页码:267-272 |
| 关键词 | NMR H-1 C-13 P-31 phosphinates methylation enzymatic reaction mechanisms cobalamin radical S-adenosyl- l-methionine |
| 通讯作者 | Hu,KF (reprint author),Chinese Acad Sci,Kunming Inst Bot,State Key Lab Phytochem & Plant Resources West Ch,Kunming 650201,Yunnan,Peoples R China. ; kaifenghu@mail.kib.ac.cn ; susan_wang@wsu.edu |
| 英文摘要 | The biochemical mechanism for the formation of the C-P-C bond sequence found in l-phosphinothricin, a natural product with antibiotic and herbicidal activity, remains unclear. To obtain further insight into the catalytic mechanism of PhpK, the P-methyltransferase responsible for the formation of the second C-P bond in l-phosphinothricin, we utilized a combination of stable isotopes and two-dimensional nuclear magnetic resonance spectroscopy. Exploiting the newly emerged Bruker QCI probe (Bruker Corp.), we specifically designed and ran a C-13-P-31 multiple quantum H-1-C-13-P-31 (HCP) experiment in H-1-P-31 two-dimensional mode directly on a PhpK-catalyzed reaction mixture using (CH3)-C-13-labeled methylcobalamin as the methyl group donor. This method is particularly advantageous because minimal sample purification is needed to maximize product visualization. The observed 3:1:1:3 multiplet specifically and unequivocally illustrates direct bond formation between (CH3)-C-13 and P-31. Related nuclear magnetic resonance experiments based upon these principles may be designed for the study of enzymatic and/or synthetic chemical reaction mechanisms. Copyright (c) 2015 John Wiley & Sons, Ltd. |
| 学科主题 | Chemistry, Multidisciplinary; Chemistry, Physical; Spectroscopy |
| 类目[WOS] | Chemistry, Multidisciplinary ; Chemistry, Physical ; Spectroscopy |
| 研究领域[WOS] | Chemistry ; Spectroscopy |
| 关键词[WOS] | TUBERCULOSIS GLUTAMINE-SYNTHETASE ; NATURAL-PRODUCTS ; RADICAL SAM ; BIALAPHOS SF-1293 ; BIOSYNTHESIS ; PHOSPHONATE ; PHOSPHINOTHRICIN ; METHYLATION ; RNA ; MECHANISM |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000351636200004 |
| 源URL | [http://ir.kib.ac.cn/handle/151853/20585]  |
| 专题 | 昆明植物研究所_植物化学与西部植物资源持续利用国家重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Kunming Inst Bot, State Key Lab Phytochem & Plant Resources West Ch, Kunming 650201, Yunnan, Peoples R China 2.Univ Wisconsin, Dept Biochem, Natl Magnet Resonance Facil Madison, Madison, WI 53706 USA 3.Washington State Univ, Sch Mol Biosci, Coll Vet Med, Pullman, WA 99164 USA 4.Virginia Polytech Inst & State Univ, Dept Biochem, Blacksburg, VA 24061 USA |
| 推荐引用方式 GB/T 7714 | Hu, Kaifeng,Werner, Williard J.,Allen, Kylie D.,et al. Investigation of enzymatic C-P bond formation using multiple quantum HCP nuclear magnetic resonance spectroscopy[J]. MAGNETIC RESONANCE IN CHEMISTRY,2015,53(4):267-272. |
| APA | Hu, Kaifeng,Werner, Williard J.,Allen, Kylie D.,&Wang, Susan C..(2015).Investigation of enzymatic C-P bond formation using multiple quantum HCP nuclear magnetic resonance spectroscopy.MAGNETIC RESONANCE IN CHEMISTRY,53(4),267-272. |
| MLA | Hu, Kaifeng,et al."Investigation of enzymatic C-P bond formation using multiple quantum HCP nuclear magnetic resonance spectroscopy".MAGNETIC RESONANCE IN CHEMISTRY 53.4(2015):267-272. |
入库方式： OAI收割
来源：昆明植物研究所
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