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The Application of Transient-State Kinetic Isotope Effects to the Resolution of Mechanisms of Enzyme-Catalyzed Reactions
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Molecules 2013, 18(8), 9278-9292; doi:10.3390/molecules18089278

Advances in Kinetic Isotope Effect Measurement Techniques for Enzyme Mechanism Study

Department of Biochemistry, Case Western Reserve University School of Medicine, 10900 Euclid Ave., Cleveland, OH 44106, USA
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Received: 18 June 2013 / Revised: 22 July 2013 / Accepted: 29 July 2013 / Published: 2 August 2013
(This article belongs to the Special Issue Isotope Effects)
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Abstract

Kinetic isotope effects (KIEs) are a very powerful tool for investigating enzyme mechanisms. Precision of measurement is the most important factor for KIE determinations, especially for small heavy atom KIEs. Internal competition is commonly used to measure small KIEs on V/K. Several methods, including such as liquid scintillation counting, mass spectrometry, nuclear magnetic resonance spectroscopy and polarimetry have been used to determine KIEs. In this paper, which does not aspire to be an exhaustive review, we briefly review different experimental approaches for the measurement of KIEs on enzymatic reaction with an emphasis on newer techniques employing mass spectrometry and nuclear magnetic resonance spectrometry as well as some corresponding examples. View Full-Text
Keywords: kinetic isotope effects; measurement; mass spectrometry; nuclear magnetic resonance; liquid scintillation counting kinetic isotope effects; measurement; mass spectrometry; nuclear magnetic resonance; liquid scintillation counting
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Gu, H.; Zhang, S. Advances in Kinetic Isotope Effect Measurement Techniques for Enzyme Mechanism Study. Molecules 2013, 18, 9278-9292.

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