On-the-Fly Kinetics of Enzymatic Racemization Using Deuterium NMR in DNA-Based Chiral Oriented Media
We report the in situ and real-time monitoring of the interconversion of L- and D-alanine-d(3) by alanine racemase from Bacillus stearothermophilus directly observed by H-2 NMR spectroscopy in anisotropic phase. The enantiomers are distinguished by the difference of their H-2 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.
P361-Chan-Huot-Lesot-Pelupessy-Duma-Bodenhausen-Duchambon-Toney-Venkateswara-Reddy-Suryaprakash-Racemase-Analytical-Chemistry-85-4694-2013.pdf
restricted
673.95 KB
Adobe PDF
be38e8ef659b98833d0f63415880c540