ArticleBiochemistry2012
Hydrogen donor-acceptor fluctuations from kinetic isotope effects: a phenomenological model.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Free energy relationship analysis for temperature dependence of hydride kinetic isotope effects of NADH/NADChemical science · 2026Article
- Large Temperature Dependence of Large Kinetic Isotope Effects of Multistep Hydride Reduction ofThe Journal of organic chemistry · 2025Article
- Rigidity Analysis of Hydride Tunneling Ready States from Secondary Kinetic Isotope Effects and Hammett Correlations: Relating to the Temperature Dependence of Kinetic Isotope Effects.Journal of physical organic chemistry · 2025Article
- Structural Effects on the Hydride-Tunneling Kinetic Isotope Effects of NADH/NADThe Journal of organic chemistry · 2025Article
- Neurostimulation devices to treat Alzheimer's disease.Exploration of neuroscience · 2025Article
- Interplay of structural preorganization and conformational sampling in UDP-glucuronic acid 4-epimerase catalysis.Nature communications · 2024Article
- Study of the Effects of Remote Heavy Group Vibrations on the Temperature Dependence of Hydride Kinetic Isotope Effects of the NADH/NADACS omega · 2024Article
- Structural Effects on the Temperature Dependence of Hydride Kinetic Isotope Effects of the NADH/NADThe Journal of organic chemistry · 2024Article
- Electromagnetic Field Stimulation Therapy for Alzheimer's Disease.Neurology (Chicago, Ill.) · 2024Article
- Correlation of temperature dependence of hydride kinetic isotope effects with donor-acceptor distances in two solvents of different polarities.Organic & biomolecular chemistry · 2023Article
- Dependence of crystallographic atomic displacement parameters on temperature (25-150 K) for complexes of horse liver alcohol dehydrogenase.Acta crystallographica. Section D, Structural biology · 2022Article
- Hydride Transfer Mechanism of Enzymatic Sugar Nucleotide C2 Epimerization Probed with a Loose-Fit CDP-Glucose Substrate.ACS catalysis · 2022Article
- Multidimensional insights into the repeated electromagnetic field stimulation and biosystems interaction in aging and age-related diseases.Journal of biomedical science · 2022Review
- Evolution of Optimized Hydride Transfer Reaction and Overall Enzyme Turnover in Human Dihydrofolate Reductase.Biochemistry · 2021Article
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- Experimental and Computational Studies Delineate the Role of Asparagine 177 in Hydride Transfer for E. coli Thymidylate Synthase.ACS catalysis · 2018Article
- Protein Mass Effects on Formate Dehydrogenase.Journal of the American Chemical Society · 2017Article
- Oscillatory Enzyme Dynamics Revealed by Two-Dimensional Infrared Spectroscopy.The journal of physical chemistry letters · 2016Article
- The Effect of Protein Mass Modulation on Human Dihydrofolate Reductase.Biochemistry · 2016Article
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3 authors.
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Abstract
Kinetic isotope effects (KIEs) and their temperature dependence can probe the structural and dynamic nature of enzyme-catalyzed proton or hydride transfers. The molecular interpretation of their temperature dependence requires expensive and specialized quantum mechanics/molecular mechanics (QM/MM) calculations to provide a quantitative molecular understanding. Currently available phenomenological models use a nonadiabatic assumption that is not appropriate for most hydride and proton-transfer reactions, while others require more parameters than the experimental data justify. Here we propose a phenomenological interpretation of KIEs based on a simple method to quantitatively link the size and temperature dependence of KIEs to a conformational distribution of the catalyzed reaction. This model assumes adiabatic hydrogen tunneling, and by fitting experimental KIE data, the model yields a population distribution for fluctuations of the distance between donor and acceptor atoms. Fits to data from a variety of proton and hydride transfers catalyzed by enzymes and their mutants, as well as nonenzymatic reactions, reveal that steeply temperature-dependent KIEs indicate the presence of at least two distinct conformational populations, each with different kinetic behaviors. We present the results of these calculations for several published cases and discuss how the predictions of the calculations might be experimentally tested. This analysis does not replace molecular QM/MM investigations, but it provides a fast and accessible way to quantitatively interpret KIEs in the context of a Marcus-like model.
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