"On-the-fly" kinetics of enzymatic racemization using deuterium NMR in DNA-based chiral oriented media

Monique Chan-Huot, Philippe Lesot, Philippe Pelupessy, Luminita Duma, Geoffrey Bodenhausen, Patricia Duchambon, Michael D. Toney, U. Venkateswara Reddy, N. Suryaprakash

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

We report the in situ and real-time monitoring of the interconversion of l- and d-alanine-d3 by alanine racemase from Bacillus stearothermophilus directly observed by 2H NMR spectroscopy in anisotropic phase. The enantiomers are distinguished by the difference of their 2H quadrupolar splittings in a chiral liquid crystal containing short DNA fragments. The proof-of-principle, the reliability, and the robustness of this new method is demonstrated by the determination of the turnover rates of the enzyme using the Michaelis-Menten model.

Original languageEnglish (US)
Pages (from-to)4694-4697
Number of pages4
JournalAnalytical Chemistry
Volume85
Issue number9
DOIs
StatePublished - May 7 2013

ASJC Scopus subject areas

  • Analytical Chemistry

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    Chan-Huot, M., Lesot, P., Pelupessy, P., Duma, L., Bodenhausen, G., Duchambon, P., Toney, M. D., Reddy, U. V., & Suryaprakash, N. (2013). "On-the-fly" kinetics of enzymatic racemization using deuterium NMR in DNA-based chiral oriented media. Analytical Chemistry, 85(9), 4694-4697. https://doi.org/10.1021/ac4004002