ArticleJournal of chemical theory and computation2016
Enzymatic Kinetic Isotope Effects from First-Principles Path Sampling Calculations.
Article in Journal of chemical theory and computation, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Contribution of buried distal amino acid residues in horse liver alcohol dehydrogenase to structure and catalysis.Protein science : a publication of the Protein Society · 2018Article
- Structurally Linked Dynamics in Lactate Dehydrogenases of Evolutionarily Distinct Species.Biochemistry · 2017Article
- Targeting a Rate-Promoting Vibration with an Allosteric Mediator in Lactate Dehydrogenase.The journal of physical chemistry letters · 2016Article
- Path Sampling Methods for Enzymatic Quantum Particle Transfer Reactions.Methods in enzymology · 2016Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In this study, we develop and test a method to determine the rate of particle transfer and kinetic isotope effects in enzymatic reactions, specifically yeast alcohol dehydrogenase (YADH), from first-principles. Transition path sampling (TPS) and normal mode centroid dynamics (CMD) are used to simulate these enzymatic reactions without knowledge of their reaction coordinates and with the inclusion of quantum effects, such as zero-point energy and tunneling, on the transferring particle. Though previous studies have used TPS to calculate reaction rate constants in various model and real systems, it has not been applied to a system as large as YADH. The calculated primary H/D kinetic isotope effect agrees with previously reported experimental results, within experimental error. The kinetic isotope effects calculated with this method correspond to the kinetic isotope effect of the transfer event itself. The results reported here show that the kinetic isotope effects calculated from first-principles, purely for barrier passage, can be used to predict experimental kinetic isotope effects in enzymatic systems.
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Registered trials
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