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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2013
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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. |
format | Online Article Text |
id | pubmed-4342783 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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