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Isotope Effects as Probes for Enzyme Catalyzed Hydrogen-Transfer Reactions

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 gro...

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Detalles Bibliográficos
Autores principales: Roston, Daniel, Islam, Zahidul, Kohen, Amnon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4342783/
https://www.ncbi.nlm.nih.gov/pubmed/23673528
http://dx.doi.org/10.3390/molecules18055543
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author Roston, Daniel
Islam, Zahidul
Kohen, Amnon
author_facet Roston, Daniel
Islam, Zahidul
Kohen, Amnon
author_sort Roston, Daniel
collection PubMed
description 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.
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spelling pubmed-43427832015-02-27 Isotope Effects as Probes for Enzyme Catalyzed Hydrogen-Transfer Reactions Roston, Daniel Islam, Zahidul Kohen, Amnon Molecules Review 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. MDPI 2013-05-14 /pmc/articles/PMC4342783/ /pubmed/23673528 http://dx.doi.org/10.3390/molecules18055543 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Roston, Daniel
Islam, Zahidul
Kohen, Amnon
Isotope Effects as Probes for Enzyme Catalyzed Hydrogen-Transfer Reactions
title Isotope Effects as Probes for Enzyme Catalyzed Hydrogen-Transfer Reactions
title_full Isotope Effects as Probes for Enzyme Catalyzed Hydrogen-Transfer Reactions
title_fullStr Isotope Effects as Probes for Enzyme Catalyzed Hydrogen-Transfer Reactions
title_full_unstemmed Isotope Effects as Probes for Enzyme Catalyzed Hydrogen-Transfer Reactions
title_short Isotope Effects as Probes for Enzyme Catalyzed Hydrogen-Transfer Reactions
title_sort isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4342783/
https://www.ncbi.nlm.nih.gov/pubmed/23673528
http://dx.doi.org/10.3390/molecules18055543
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