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Molecules 2013, 18(5), 5543-5567; doi:10.3390/molecules18055543

Isotope Effects as Probes for Enzyme Catalyzed Hydrogen-Transfer Reactions

Department of Chemistry, The University of Iowa, Iowa City, IA 52242, USA
These authors contributed equally to this work.
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Received: 11 April 2013 / Revised: 30 April 2013 / Accepted: 3 May 2013 / Published: 14 May 2013
(This article belongs to the Special Issue Isotope Effects)
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Abstract

Kinetic Isotope effects (KIEs) have long served as a probe for the mechanisms of both enzymatic and solution reactions. Here, we discuss various models for the physical sources of KIEs, how experimentalists can use those models to interpret their data, and how the focus of traditional models has grown to a model that includes motion of the enzyme and quantum mechanical nuclear tunneling. We then present two case studies of enzymes, thymidylate synthase and alcohol dehydrogenase, and discuss how KIEs have shed light on the C-H bond cleavages those enzymes catalyze. We will show how the combination of both experimental and computational studies has changed our notion of how these enzymes exert their catalytic powers.
Keywords: kinetic isotope effects; Marcus-like models; alcohol dehydrogenase; thymidylate synthase; hydrogen tunneling kinetic isotope effects; Marcus-like models; alcohol dehydrogenase; thymidylate synthase; hydrogen tunneling
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Roston, D.; Islam, Z.; Kohen, A. Isotope Effects as Probes for Enzyme Catalyzed Hydrogen-Transfer Reactions. Molecules 2013, 18, 5543-5567.

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