Investigation of enzymatic C-P bond formation using multiple quantum HCP nuclear magnetic resonance spectroscopy

Copyright © 2015 John Wiley & Sons, Ltd.

Bibliographische Detailangaben
Veröffentlicht in:Magnetic resonance in chemistry : MRC. - 1985. - 53(2015), 4 vom: 14. Apr., Seite 267-72
1. Verfasser: Hu, Kaifeng (VerfasserIn)
Weitere Verfasser: Werner, Williard J, Allen, Kylie D, Wang, Susan C
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2015
Zugriff auf das übergeordnete Werk:Magnetic resonance in chemistry : MRC
Schlagworte:Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. 13C 1H 31P NMR cobalamin enzymatic reaction mechanisms mehr... methylation phosphinates radical S-adenosyl- l-methionine Aminobutyrates Carbon Isotopes Phosphorus Isotopes phosphinothricin 51276-47-2 mecobalamin BR1SN1JS2W Methyltransferases EC 2.1.1.- P-methyltransferase Vitamin B 12 P6YC3EG204
Beschreibung
Zusammenfassung:Copyright © 2015 John Wiley & Sons, Ltd.
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 (13) C-(31) P multiple quantum (1) H-(13) C-(31) P (HCP) experiment in (1) H-(31) P two-dimensional mode directly on a PhpK-catalyzed reaction mixture using (13) CH3 -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 (13) CH3 and (31) P. Related nuclear magnetic resonance experiments based upon these principles may be designed for the study of enzymatic and/or synthetic chemical reaction mechanisms
Beschreibung:Date Completed 04.12.2015
Date Revised 13.11.2018
published: Print-Electronic
Citation Status MEDLINE
ISSN:1097-458X
DOI:10.1002/mrc.4190