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Good vibrations in enzyme-catalysed reactions
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/anie.200805502openalex-snapshot
Barrier Compression Enhances an Enzymatic Hydrogen‐Transfer Reaction
inferredcites →https://doi.org/10.1002/anie.200900086openalex-snapshot
Solvent‐Slaved Protein Motions Accompany Proton but Not Hydride Tunneling in Light‐Activated Protochlorophyllide Oxidoreductase
inferredcites →https://doi.org/10.1002/anie.201006668openalex-snapshot
How Does Pressure Affect Barrier Compression and Isotope Effects in an Enzymatic Hydrogen Tunneling Reaction?
inferredcites →https://doi.org/10.1002/cbic.200900071openalex-snapshot
Parallel Pathways and Free‐Energy Landscapes for Enzymatic Hydride Transfer Probed by Hydrostatic Pressure
inferredcites →https://doi.org/10.1002/chem.201000635openalex-snapshot
Do Dynamic Effects Play a Significant Role in Enzymatic Catalysis? A Theoretical Analysis of Formate Dehydrogenase
inferredcites →https://doi.org/10.1002/poc.1633openalex-snapshot
Enzymatic tunneling and kinetic isotope effects: chemistry at the crossroads
inferredcites →https://doi.org/10.1002/poc.1653openalex-snapshot
Probing active site geometry using high pressure and secondary isotope effects in an enzyme‐catalysed ‘deep’ H‐tunnelling reaction
inferredcites →https://doi.org/10.1002/poc.1676openalex-snapshot
Tunneling in enzymatic and nonenzymatic hydrogen transfer reactions
inferredcites →https://doi.org/10.1002/prot.22654openalex-snapshot
At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?
inferredcites →https://doi.org/10.1007/978-1-4899-2891-7openalex-snapshot
The Tunnel Effect in Chemistry
inferredcites →https://doi.org/10.1016/j.abb.2004.03.013openalex-snapshot
Hydrogen tunneling in quinoproteins
inferredcites →https://doi.org/10.1016/j.bpj.2009.09.045openalex-snapshot
Barrier Compression and Its Contribution to Both Classical and Quantum Mechanical Aspects of Enzyme Catalysis
inferredcites →https://doi.org/10.1016/j.febslet.2010.04.062openalex-snapshot
Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issues
inferredcites →https://doi.org/10.1021/bi100761xopenalex-snapshot
The Temperature Dependence of the Kinetic Isotope Effects of Dihydrofolate Reductase from Thermotoga maritima Is Influenced by Intersubunit Interactions
inferredcites →https://doi.org/10.1021/bi700201wopenalex-snapshot
The Catalytic Effect of Dihydrofolate Reductase and Its Mutants Is Determined by Reorganization Energies
inferredcites →https://doi.org/10.1021/bi701690uopenalex-snapshot
Catalysis by the Isolated Tryptophan Tryptophylquinone-Containing Subunit of Aromatic Amine Dehydrogenase Is Distinct from Native Enzyme and Synthetic Model Compounds and Allows Further Probing of TTQ Mechanism
inferredcites →https://doi.org/10.1021/bi800049zopenalex-snapshot
Free-Energy Landscape of Enzyme Catalysis
inferredcites →https://doi.org/10.1021/bi8005972openalex-snapshot
Incorporation of Hydrostatic Pressure into Models of Hydrogen Tunneling Highlights a Role for Pressure-Modulated Promoting Vibrations
inferredcites →https://doi.org/10.1021/cr0503052openalex-snapshot
Computational and Theoretical Methods to Explore the Relation between Enzyme Dynamics and Catalysis
inferredcites →https://doi.org/10.1021/cr1001035openalex-snapshot
Update 1 of: Tunneling and Dynamics in Enzymatic Hydride Transfer
inferredcites →https://doi.org/10.1021/ja00540a008openalex-snapshot
An empirical valence bond approach for comparing reactions in solutions and in enzymes
inferredcites →https://doi.org/10.1021/ja012205topenalex-snapshot
Temperature-Dependent Isotope Effects in Soybean Lipoxygenase-1: Correlating Hydrogen Tunneling with Protein Dynamics
inferredcites →https://doi.org/10.1021/ja017146yopenalex-snapshot
Identification of a Protein-Promoting Vibration in the Reaction Catalyzed by Horse Liver Alcohol Dehydrogenase
inferredcites →https://doi.org/10.1021/ja030120hopenalex-snapshot
The First Experimental Test of the Hypothesis that Enzymes Have Evolved To Enhance Hydrogen Tunneling
inferredcites →https://doi.org/10.1021/ja035692gopenalex-snapshot
Evidence for Environmentally Coupled Hydrogen Tunneling during Dihydrofolate Reductase Catalysis
inferredcites →https://doi.org/10.1021/ja039606oopenalex-snapshot
Proton-Coupled Electron Transfer in Soybean Lipoxygenase
inferredcites →https://doi.org/10.1021/ja0457563openalex-snapshot
Promoting Vibrations in Human Purine Nucleoside Phosphorylase. A Molecular Dynamics and Hybrid Quantum Mechanical/Molecular Mechanical Study
inferredcites →https://doi.org/10.1021/ja0614619openalex-snapshot
α-Secondary Isotope Effects as Probes of “Tunneling-Ready” Configurations in Enzymatic H-Tunneling: Insight from Environmentally Coupled Tunneling Models
inferredcites →https://doi.org/10.1021/ja0667211openalex-snapshot
Proton-Coupled Electron Transfer in Soybean Lipoxygenase: Dynamical Behavior and Temperature Dependence of Kinetic Isotope Effects
inferredcites →https://doi.org/10.1021/ja074463hopenalex-snapshot
Mutagenesis of Morphinone Reductase Induces Multiple Reactive Configurations and Identifies Potential Ambiguity in Kinetic Analysis of Enzyme Tunneling Mechanisms
inferredcites →https://doi.org/10.1021/ja1048048openalex-snapshot
Direct Analysis of Donor−Acceptor Distance and Relationship to Isotope Effects and the Force Constant for Barrier Compression in Enzymatic H-Tunneling Reactions
inferredcites →https://doi.org/10.1021/ja1114369openalex-snapshot
Temperature Dependence of the Kinetic Isotope Effects in Thymidylate Synthase. A Theoretical Study
inferredcites →https://doi.org/10.1021/ja800471fopenalex-snapshot
Deep Tunneling Dominates the Biologically Important Hydride Transfer Reaction from NADH to FMN in Morphinone Reductase
inferredcites →https://doi.org/10.1021/ja908469mopenalex-snapshot
Evidence To Support the Hypothesis That Promoting Vibrations Enhance the Rate of an Enzyme Catalyzed H-Tunneling Reaction
inferredcites →https://doi.org/10.1021/jp0364349openalex-snapshot
Donor−Acceptor Distance and Protein Promoting Vibration Coupling to Hydride Transfer: A Possible Mechanism for Kinetic Control in Isozymes of Human Lactate Dehydrogenase
inferredcites →https://doi.org/10.1021/jp051184copenalex-snapshot
Small Temperature Dependence of the Kinetic Isotope Effect for the Hydride Transfer Reaction Catalyzed by Escherichia coli Dihydrofolate Reductase
inferredcites →https://doi.org/10.1021/jp066276wopenalex-snapshot
Proton Tunneling in Aromatic Amine Dehydrogenase is Driven by a Short-Range Sub-Picosecond Promoting Vibration: Consistency of Simulation and Theory with Experiment
inferredcites →https://doi.org/10.1021/jp070938fopenalex-snapshot
Origin of the Temperature Dependence of Isotope Effects in Enzymatic Reactions: The Case of Dihydrofolate Reductase
inferredcites →https://doi.org/10.1038/20981openalex-snapshot
Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase
inferredcites →https://doi.org/10.1038/363320a0openalex-snapshot
Visualization of coherent nuclear motion in a membrane protein by femtosecond spectroscopy
inferredcites →https://doi.org/10.1038/nature06407openalex-snapshot
A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
inferredcites →https://doi.org/10.1038/nature06410openalex-snapshot
Intrinsic motions along an enzymatic reaction trajectory
inferredcites →https://doi.org/10.1038/nature06522openalex-snapshot
Dynamic personalities of proteins
inferredcites →https://doi.org/10.1038/nature07354openalex-snapshot
Conformational changes in an ultrafast light-driven enzyme determine catalytic activity
inferredcites →https://doi.org/10.1038/nchembio.202openalex-snapshot
Enzymatic transition states and dynamic motion in barrier crossing
inferredcites →https://doi.org/10.1039/9781847559975openalex-snapshot
Quantum Tunnelling in Enzyme-Catalysed Reactions
inferredcites →https://doi.org/10.1039/9781847559975-00036openalex-snapshot
Quantum Catalysis in Enzymes
inferredcites →https://doi.org/10.1042/bst0360016openalex-snapshot
Atomistic insight into the origin of the temperature-dependence of kinetic isotope effects and H-tunnelling in enzyme systems is revealed through combined experimental studies and biomolecular simulation
inferredcites →https://doi.org/10.1073/pnas.052005999openalex-snapshot
Network of coupled promoting motions in enzyme catalysis
inferredcites →https://doi.org/10.1073/pnas.0606976103openalex-snapshot
Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase
inferredcites →https://doi.org/10.1073/pnas.0608408104openalex-snapshot
Promoting motions in enzyme catalysis probed by pressure studies of kinetic isotope effects
inferredcites →https://doi.org/10.1073/pnas.0704304104openalex-snapshot
Reaction coordinate of an enzymatic reaction revealed by transition path sampling
inferredcites →https://doi.org/10.1073/pnas.0710643105openalex-snapshot
Enzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1
inferredcites →https://doi.org/10.1073/pnas.0808413105openalex-snapshot
Atomic detail of chemical transformation at the transition state of an enzymatic reaction
inferredcites →https://doi.org/10.1073/pnas.0909150106openalex-snapshot
Enzyme millisecond conformational dynamics do not catalyze the chemical step
inferredcites →https://doi.org/10.1073/pnas.0911416106openalex-snapshot
Differential quantum tunneling contributions in nitroalkane oxidase catalyzed and the uncatalyzed proton transfer reaction
inferredcites →https://doi.org/10.1073/pnas.0912190107openalex-snapshot
Characterizing the dynamics of functionally relevant complexes of formate dehydrogenase
inferredcites →https://doi.org/10.1073/pnas.0914163107openalex-snapshot
Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands
inferredcites →https://doi.org/10.1073/pnas.1002180107openalex-snapshot
Role of conformation transitions in adenylate kinase
inferredcites →https://doi.org/10.1073/pnas.1106397108openalex-snapshot
Dynamics and dissipation in enzyme catalysis
inferredcites →https://doi.org/10.1073/pnas.1111252108openalex-snapshot
Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions
inferredcites →https://doi.org/10.1074/jbc.m111.219626openalex-snapshot
A Twin-track Approach Has Optimized Proton and Hydride Transfer by Dynamically Coupled Tunneling during the Evolution of Protochlorophyllide Oxidoreductase
inferredcites →https://doi.org/10.1074/jbc.m808548200openalex-snapshot
Nuclear Quantum Tunneling in the Light-activated Enzyme Protochlorophyllide Oxidoreductase
inferredcites →https://doi.org/10.1098/rsif.2008.0068.focusopenalex-snapshot
The enzyme aromatic amine dehydrogenase induces a substrate conformation crucial for promoting vibration that significantly reduces the effective potential energy barrier to proton transfer
inferredcites →https://doi.org/10.1111/j.1742-4658.2009.07121.xopenalex-snapshot
Structural and mechanistic aspects of flavoproteins: probes of hydrogen tunnelling
inferredcites →https://doi.org/10.1126/science.1126002openalex-snapshot
Atomic Description of an Enzyme Reaction Dominated by Proton Tunneling
inferredcites →https://doi.org/10.1126/science.1130258openalex-snapshot
The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis
inferredcites →https://doi.org/10.1126/science.1198542openalex-snapshot
A Dynamic Knockout Reveals That Conformational Fluctuations Influence the Chemical Step of Enzyme Catalysis
inferredcites →https://doi.org/10.1139/cjc-77-5-6-1085openalex-snapshot
Proton and hydrogen atom tunnelling in hydrolytic and redox enzyme catalysis
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Protein Motions Are Coupled to the Reaction Chemistry in Coenzyme B12‐Dependent Ethanolamine Ammonia Lyase
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Tunneling Governs Intramolecular Proton Transfer in Thiotropolone at Room Temperature
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A Biophysical Perspective on Enzyme Catalysis
inferred← citeshttps://doi.org/10.1021/acs.biochem.9b00574openalex-snapshot
Replication of the Enzymatic Temperature Dependency of the Primary Hydride Kinetic Isotope Effects in Solution: Caused by the Protein-Controlled Rigidity of the Donor–Acceptor Centers?
inferred← citeshttps://doi.org/10.1021/acs.chemrev.5b00340openalex-snapshot
Manganese Compounds as Water-Oxidizing Catalysts: From the Natural Water-Oxidizing Complex to Nanosized Manganese Oxide Structures
inferred← citeshttps://doi.org/10.1021/acs.jcim.3c00194openalex-snapshot
The Conformational Transitions and Dynamics of Burkholderia cepacia Lipase Regulated by Water–Oil Interfaces
inferred← citeshttps://doi.org/10.1021/acs.jcim.8b00946openalex-snapshot
Protein–Ligand Complexes as Constrained Dynamical Systems
inferred← citeshttps://doi.org/10.1021/acs.joc.3c02562openalex-snapshot
Structural Effects on the Temperature Dependence of Hydride Kinetic Isotope Effects of the NADH/NAD+ Model Reactions in Acetonitrile: Charge-Transfer Complex Tightness Is a Key
inferred← citeshttps://doi.org/10.1021/acs.jpca.1c05879openalex-snapshot
Probing Hydrogen-Bonding Interactions within Phenol-Benzimidazole Proton-Coupled Electron Transfer Model Complexes with Cryogenic Ion Vibrational Spectroscopy
inferred← citeshttps://doi.org/10.1021/acs.jpca.3c00524openalex-snapshot
Unraveling the Vibrational Spectral Signatures of a Dislocated H Atom in Model Proton-Coupled Electron Transfer Dyad Systems
inferred← citeshttps://doi.org/10.1021/acs.jpca.6b03571openalex-snapshot
Computational Replication of the Primary Isotope Dependence of Secondary Kinetic Isotope Effects in Solution Hydride-Transfer Reactions: Supporting the Isotopically Different Tunneling Ready State Conformations
inferred← citeshttps://doi.org/10.1021/acs.jpca.7b00539openalex-snapshot
Proton-Coupled Electron Transfer and the “Linear Approximation” for Coupling to the Donor–Acceptor Distance Fluctuations
inferred← citeshttps://doi.org/10.1021/acs.jpcb.0c04929openalex-snapshot
Ultrafast Vibrational Energy Transfer between Protein and Cofactor in a Flavoenzyme
inferred← citeshttps://doi.org/10.1021/acs.jpcb.0c05725openalex-snapshot
Role of Protein Motions in Catalysis by Formate Dehydrogenase
inferred← citeshttps://doi.org/10.1021/acs.jpcb.0c10318openalex-snapshot
Temperature-Dependent Kinetic Isotope Effects in R67 Dihydrofolate Reductase from Path-Integral Simulations
inferred← citeshttps://doi.org/10.1021/acs.jpcb.2c03251openalex-snapshot
Transition Path Sampling Based Calculations of Free Energies for Enzymatic Reactions: The Case of Human Methionine Adenosyl Transferase and Plasmodium vivax Adenosine Deaminase
inferred← citeshttps://doi.org/10.1021/acs.jpcb.2c05112openalex-snapshot
Comparison of the Role of Protein Dynamics in Catalysis by Dihydrofolate Reductase from E. coli and H. sapiens
inferred← citeshttps://doi.org/10.1021/acs.jpcb.3c05307openalex-snapshot
Conformational Dynamics in Proteins: Entangled Slow Fluctuations and Nonequilibrium Reaction Events
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b06758openalex-snapshot
Isotopic Effects on Covalent Bond Confined in a Penetrable Sphere
inferred← citeshttps://doi.org/10.1021/acs.jpcb.6b10245openalex-snapshot
Collective Excitations in Protein as a Measure of Balance Between its Softness and Rigidity
inferred← citeshttps://doi.org/10.1021/acs.jpcb.7b05319openalex-snapshot
Incorporating Fast Protein Dynamics into Enzyme Design: A Proposed Mutant Aromatic Amine Dehydrogenase
inferred← citeshttps://doi.org/10.1021/acs.jpcb.7b05570openalex-snapshot
Tunneling Kinetics and Nonadiabatic Proton-Coupled Electron Transfer in Proteins: The Effect of Electric Fields and Anharmonic Donor–Acceptor Interactions
inferred← citeshttps://doi.org/10.1021/acs.jpcb.7b06892openalex-snapshot
Ab Initio QM/MM Modeling of the Rate-Limiting Proton Transfer Step in the Deamination of Tryptamine by Aromatic Amine Dehydrogenase
inferred← citeshttps://doi.org/10.1021/acs.jpcb.7b06985openalex-snapshot
Proton Network Flexibility Enables Robustness and Large Electric Fields in the Ketosteroid Isomerase Active Site
inferred← citeshttps://doi.org/10.1021/acs.jpcc.0c03703openalex-snapshot
Tuning Quantum Dots Coupling Using Organic Linkers with Different Vibrational Modes
inferred← citeshttps://doi.org/10.1021/acs.jpclett.1c01453openalex-snapshot
Temperature-Dependent Low-Frequency Modes in the Active Site of Bovine Carbonic Anhydrase II Probed by 2D-IR Spectroscopy
inferred← citeshttps://doi.org/10.1021/acs.jpclett.6c01422openalex-snapshot
Detecting Vibrational Energy Transfer into an Enzyme Active Site via a Transition State Analog
inferred← citeshttps://doi.org/10.1021/acs.jpclett.8b03607openalex-snapshot
Conformational Excitation and Nonequilibrium Transition Facilitate Enzymatic Reactions: Application to Pin1 Peptidyl–Prolyl Isomerase
inferred← citeshttps://doi.org/10.1021/acs.nanolett.4c01137openalex-snapshot
DNA Framework–Programmed Nanoscale Enzyme Assemblies
inferred← citeshttps://doi.org/10.1021/acs.nanolett.5c03728openalex-snapshot
Nanoscale Temperature Increases Are Not Required for Molecular Stimulation Using Nanoparticles under Radiofrequency Magnetic Fields: A Thermal Energy Flux Mechanism of Remote Enzyme Stimulation
inferred← citeshttps://doi.org/10.1021/acscatal.1c04679openalex-snapshot
Chemical Mapping Exposes the Importance of Active Site Interactions in Governing the Temperature Dependence of Enzyme Turnover
inferred← citeshttps://doi.org/10.1021/acscatal.2c00257openalex-snapshot
Hydride Transfer Mechanism of Enzymatic Sugar Nucleotide C2 Epimerization Probed with a Loose-Fit CDP-Glucose Substrate
inferred← citeshttps://doi.org/10.1021/acscatal.3c02687openalex-snapshot
Temporal Resolution of Activity-Related Solvation Dynamics in the TIM Barrel Enzyme Murine Adenosine Deaminase
inferred← citeshttps://doi.org/10.1021/acscatal.4c00439openalex-snapshot
Identification of the Thermal Activation Network in Human 15-Lipoxygenase-2: Divergence from Plant Orthologs and Its Relationship to Hydrogen Tunneling Activation Barriers
inferred← citeshttps://doi.org/10.1021/acscatal.4c01446openalex-snapshot
Substrate Turnover Dynamics Guide Ketol-Acid Reductoisomerase Redesign for Increased Specific Activity
inferred← citeshttps://doi.org/10.1021/acscatal.5b00331openalex-snapshot
Network of Remote and Local Protein Dynamics in Dihydrofolate Reductase Catalysis
inferred← citeshttps://doi.org/10.1021/acscatal.5b01332openalex-snapshot
Activation of Two Sequential H Transfers in the Thymidylate Synthase Catalyzed Reaction
inferred← citeshttps://doi.org/10.1021/acscatal.5c03307openalex-snapshot
The Uncatalyzed Reduction of Flavin Mononucleotide (FMN) by Nicotinamide Adenine Dinucleotide (NADH): A Reference Reaction for Catalysis by NAD(P)H-Dependent Flavoenzymes
inferred← citeshttps://doi.org/10.1021/acscatal.6b01280openalex-snapshot
Correlating Calmodulin Landscapes with Chemical Catalysis in Neuronal Nitric Oxide Synthase using Time-Resolved FRET and a 5-Deazaflavin Thermodynamic Trap
inferred← citeshttps://doi.org/10.1021/acscatal.7b00201openalex-snapshot
Convergence of Theory and Experiment on the Role of Preorganization, Quantum Tunneling, and Enzyme Motions into Flavoenzyme-Catalyzed Hydride Transfer
inferred← citeshttps://doi.org/10.1021/acscatal.7b04199openalex-snapshot
Origin of Enzymatic Kinetic Isotope Effects in Human Purine Nucleoside Phosphorylase
inferred← citeshttps://doi.org/10.1021/acscatal.8b02810openalex-snapshot
Nonequivalence of Second Sphere “Noncatalytic” Residues in Pentaerythritol Tetranitrate Reductase in Relation to Local Dynamics Linked to H-Transfer in Reactions with NADH and NADPH Coenzymes
inferred← citeshttps://doi.org/10.1021/acscatal.8b03363openalex-snapshot
The Catalytic Mechanism of DNA and RNA Polymerases
inferred← citeshttps://doi.org/10.1021/acscatal.8b04045openalex-snapshot
Electrostatics as the Driving Force Behind the Catalytic Function of the Monoamine Oxidase A Enzyme Confirmed by Quantum Computations
inferred← citeshttps://doi.org/10.1021/acscatal.9b00174openalex-snapshot
Equatorial Active Site Compaction and Electrostatic Reorganization in Catechol- O -methyltransferase
inferred← citeshttps://doi.org/10.1021/acscatal.9b03345openalex-snapshot
Oscillatory Active-Site Motions Correlate with Kinetic Isotope Effects in Formate Dehydrogenase
inferred← citeshttps://doi.org/10.1021/acsomega.0c00715openalex-snapshot
Structural Evidence for Isoform-Selective Allosteric Inhibition of Lactate Dehydrogenase A
inferred← citeshttps://doi.org/10.1021/acsomega.0c01900openalex-snapshot
Substrate Binding Stiffens Aspartate Aminotransferase by Altering the Enzyme Picosecond Vibrational Dynamics
inferred← citeshttps://doi.org/10.1021/acsomega.0c03472openalex-snapshot
Multiple Reaction Pathways in the Morphinone Reductase-Catalyzed Hydride Transfer Reaction
inferred← citeshttps://doi.org/10.1021/acsomega.3c09084openalex-snapshot
Perspectives on Computational Enzyme Modeling: From Mechanisms to Design and Drug Development
inferred← citeshttps://doi.org/10.1021/acsomega.4c02383openalex-snapshot
Study of the Effects of Remote Heavy Group Vibrations on the Temperature Dependence of Hydride Kinetic Isotope Effects of the NADH/NAD+ Model Reactions
inferred← citeshttps://doi.org/10.1021/acssuschemeng.3c07864openalex-snapshot
High-Concentration Alkane Output via In Situ Thermal-Assisted Photocatalytic Decarboxylation of Biomass-Derived Fatty Acid
inferred← citeshttps://doi.org/10.1021/ar500322sopenalex-snapshot
Role of Dynamics in Enzyme Catalysis: Substantial versus Semantic Controversies
inferred← citeshttps://doi.org/10.1021/bi3001352openalex-snapshot
Active Site Hydrophobic Residues Impact Hydrogen Tunneling Differently in a Thermophilic Alcohol Dehydrogenase at Optimal versus Nonoptimal Temperatures
inferred← citeshttps://doi.org/10.1021/bi3008593openalex-snapshot
Molecular Modeling of the Reaction Pathway and Hydride Transfer Reactions of HMG-CoA Reductase
inferred← citeshttps://doi.org/10.1021/bi301515jopenalex-snapshot
Catalytic Efficiency of Enzymes: A Theoretical Analysis
inferred← citeshttps://doi.org/10.1021/bi301559qopenalex-snapshot
Connecting Protein Conformational Dynamics with Catalytic Function As Illustrated in Dihydrofolate Reductase
inferred← citeshttps://doi.org/10.1021/bi3016873openalex-snapshot
Investigation of NADH Binding, Hydride Transfer, and NAD+ Dissociation during NADH Oxidation by Mitochondrial Complex I Using Modified Nicotinamide Nucleotides
inferred← citeshttps://doi.org/10.1021/bi400215wopenalex-snapshot
Combined Quantum Mechanics/Molecular Mechanics (QM/MM) Methods in Computational Enzymology
inferred← citeshttps://doi.org/10.1021/bi500215aopenalex-snapshot
Energy Landscape of the Michaelis Complex of Lactate Dehydrogenase: Relationship to Catalytic Mechanism
inferred← citeshttps://doi.org/10.1021/cr300463yopenalex-snapshot
Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO 2 Fixation
inferred← citeshttps://doi.org/10.1021/ct3010694openalex-snapshot
Excited-State Tautomerization of 7-Azaindole in Nonpolar Solution: A Theoretical Study Based on Liquid-Phase Potential Surfaces of Mean Force
inferred← citeshttps://doi.org/10.1021/ct5000742openalex-snapshot
How Accurate Are Transition States from Simulations of Enzymatic Reactions?
inferred← citeshttps://doi.org/10.1021/ic500284qopenalex-snapshot
Uncovering the Role of Intra- and Intermolecular Motion in Frustrated Lewis Acid/Base Chemistry: Ab Initio Molecular Dynamics Study of CO2 Binding by Phosphorus/Boron Frustrated Lewis Pair [tBu3P/B(C6F5)3]
inferred← citeshttps://doi.org/10.1021/ja3024115openalex-snapshot
Pressure Effects on Enzyme-Catalyzed Quantum Tunneling Events Arise from Protein-Specific Structural and Dynamic Changes
inferred← citeshttps://doi.org/10.1021/ja307859mopenalex-snapshot
A Remote Mutation Affects the Hydride Transfer by Disrupting Concerted Protein Motions in Thymidylate Synthase
inferred← citeshttps://doi.org/10.1021/ja308295popenalex-snapshot
Electrostatically Guided Dynamics—The Root of Fidelity in a Promiscuous Terpene Synthase?
inferred← citeshttps://doi.org/10.1021/ja309286ropenalex-snapshot
Enzymatic Single-Molecule Kinetic Isotope Effects
inferred← citeshttps://doi.org/10.1021/ja311277kopenalex-snapshot
Fast Protein Motions Are Coupled to Enzyme H-Transfer Reactions
inferred← citeshttps://doi.org/10.1021/ja400761xopenalex-snapshot
Mg2+ Binds to the Surface of Thymidylate Synthase and Affects Hydride Transfer at the Interior Active Site
inferred← citeshttps://doi.org/10.1021/ja411998hopenalex-snapshot
Extension and Limits of the Network of Coupled Motions Correlated to Hydride Transfer in Dihydrofolate Reductase
inferred← citeshttps://doi.org/10.1021/ja502673hopenalex-snapshot
Different Dynamical Effects in Mesophilic and Hyperthermophilic Dihydrofolate Reductases
inferred← citeshttps://doi.org/10.1021/ja502726sopenalex-snapshot
Extremely Elevated Room-Temperature Kinetic Isotope Effects Quantify the Critical Role of Barrier Width in Enzymatic C–H Activation
inferred← citeshttps://doi.org/10.1021/jacs.0c09106openalex-snapshot
Proton-Coupled Electron Transfer Guidelines, Fair and Square
inferred← citeshttps://doi.org/10.1021/jacs.5b03085openalex-snapshot
Steric Effects on the Primary Isotope Dependence of Secondary Kinetic Isotope Effects in Hydride Transfer Reactions in Solution: Caused by the Isotopically Different Tunneling Ready State Conformations?
inferred← citeshttps://doi.org/10.1021/jacs.5c21821openalex-snapshot
Proton-Coupled Electron Transfer Governs Heterogeneous Fenton-like Reactivity: Modulation of Surface O–H Bond Dissociation Free Energy and Proton Activity
inferred← citeshttps://doi.org/10.1021/jacs.6b05625openalex-snapshot
Donor–Acceptor Distance Sampling Enhances the Performance of “Better than Nature” Nicotinamide Coenzyme Biomimetics
inferred← citeshttps://doi.org/10.1021/jacs.6b07852openalex-snapshot
Untangling Heavy Protein and Cofactor Isotope Effects on Enzyme-Catalyzed Hydride Transfer
inferred← citeshttps://doi.org/10.1021/jacs.6b11856openalex-snapshot
13C ENDOR Spectroscopy of Lipoxygenase–Substrate Complexes Reveals the Structural Basis for C–H Activation by Tunneling
inferred← citeshttps://doi.org/10.1021/jacs.6b12531openalex-snapshot
Isolating the Effects of the Proton Tunneling Distance on Proton-Coupled Electron Transfer in a Series of Homologous Tyrosine-Base Model Compounds
inferred← citeshttps://doi.org/10.1021/jacs.7b08359openalex-snapshot
Protein Mass Effects on Formate Dehydrogenase
inferred← citeshttps://doi.org/10.1021/jacs.7b08418openalex-snapshot
Origins of Enzyme Catalysis: Experimental Findings for C–H Activation, New Models, and Their Relevance to Prevailing Theoretical Constructs
inferred← citeshttps://doi.org/10.1021/jacs.7b12369openalex-snapshot
Activity-Related Microsecond Dynamics Revealed by Temperature-Jump Förster Resonance Energy Transfer Measurements on Thermophilic Alcohol Dehydrogenase
inferred← citeshttps://doi.org/10.1021/jacs.7b13655openalex-snapshot
Insights on the Origin of Catalysis on Glycine N -Methyltransferase from Computational Modeling
inferred← citeshttps://doi.org/10.1021/jacs.8b10992openalex-snapshot
Biophysical Characterization of a Disabled Double Mutant of Soybean Lipoxygenase: The “Undoing” of Precise Substrate Positioning Relative to Metal Cofactor and an Identified Dynamical Network
inferred← citeshttps://doi.org/10.1021/jacs.9b03663openalex-snapshot
A Transient and Flexible Cation?? Interaction Promotes Hydrolysis of Nucleic Acids in DNA and RNA Nucleases
inferred← citeshttps://doi.org/10.1021/jacs.9b04515openalex-snapshot
Optimization of the Turnover in Artificial Enzymes via Directed Evolution Results in the Coupling of Protein Dynamics to Chemistry
inferred← citeshttps://doi.org/10.1021/jacs.9b08189openalex-snapshot
Elucidating Proton-Coupled Electron Transfer Mechanisms of Metal Hydrides with Free Energy- and Pressure-Dependent Kinetics
inferred← citeshttps://doi.org/10.1021/jo300879ropenalex-snapshot
A Model Reaction Assesses Contribution of H-Tunneling and Coupled Motions to Enzyme Catalysis
inferred← citeshttps://doi.org/10.1021/jo402650aopenalex-snapshot
Computational Replication of the Abnormal Secondary Kinetic Isotope Effects in a Hydride Transfer Reaction in Solution with a Motion Assisted H-Tunneling Model
inferred← citeshttps://doi.org/10.1021/jp307556jopenalex-snapshot
Quantum Variational Transition State Theory for Hydrogen Tunneling in Enzyme Catalysis
inferred← citeshttps://doi.org/10.1021/jp400160zopenalex-snapshot
Isotopic Dependence of Excited-State Proton-Tunneling Dynamics in Tropolone Probed by Polarization-Resolved Degenerate Four-Wave Mixing Spectroscopy
inferred← citeshttps://doi.org/10.1021/jp402727bopenalex-snapshot
Quantum Confinement of the Covalent Bond beyond the Born–Oppenheimer Approximation
inferred← citeshttps://doi.org/10.1021/jp505746xopenalex-snapshot
Linking Electrostatic Effects and Protein Motions in Enzymatic Catalysis. A Theoretical Analysis of Catechol O-Methyltransferase
inferred← citeshttps://doi.org/10.1021/jp506373qopenalex-snapshot
Evolution Alters the Enzymatic Reaction Coordinate of Dihydrofolate Reductase
inferred← citeshttps://doi.org/10.1021/jp5082033openalex-snapshot
How Short is the Strongest Hydrogen Bond in the Proton-Bound Homodimers of Pyridine Derivatives?
inferred← citeshttps://doi.org/10.1038/nchem.1660openalex-snapshot
Studying the role of protein dynamics in an SN2 enzyme reaction using free-energy surfaces and solvent coordinates
inferred← citeshttps://doi.org/10.1038/nchem.2527openalex-snapshot
Wide-dynamic-range kinetic investigations of deep proton tunnelling in proteins
inferred← citeshttps://doi.org/10.1038/ncomms4012openalex-snapshot
Non-classicality of the molecular vibrations assisting exciton energy transfer at room temperature
inferred← citeshttps://doi.org/10.1038/ncomms4999openalex-snapshot
Terahertz underdamped vibrational motion governs protein-ligand binding in solution
inferred← citeshttps://doi.org/10.1038/s41467-020-20212-1openalex-snapshot
Dynamical strengthening of covalent and non-covalent molecular interactions by nuclear quantum effects at finite temperature
inferred← citeshttps://doi.org/10.1038/s41467-025-59645-xopenalex-snapshot
Fast product release requires active-site water dynamics in carbonic anhydrase
inferred← citeshttps://doi.org/10.1038/s41557-018-0076-xopenalex-snapshot
Accelerating proton-coupled electron transfer of metal hydrides in catalyst model reactions
inferred← citeshttps://doi.org/10.1038/s41565-020-0672-yopenalex-snapshot
Optomechanical detection of vibration modes of a single bacterium
inferred← citeshttps://doi.org/10.1038/s41598-017-13990-0openalex-snapshot
Zymophore identification enables the discovery of novel phenylalanine ammonia lyase enzymes
inferred← citeshttps://doi.org/10.1038/s41598-019-48905-8openalex-snapshot
Universality of fold-encoded localized vibrations in enzymes
inferred← citeshttps://doi.org/10.1038/s41598-020-74439-5openalex-snapshot
The physical origin of rate promoting vibrations in enzymes revealed by structural rigidity
inferred← citeshttps://doi.org/10.1038/s41929-026-01478-yopenalex-snapshot
A geometric foundation model for enzyme retrieval with evolutionary insights
inferred← citeshttps://doi.org/10.1039/c2cc36110hopenalex-snapshot
Imbalanced tunneling ready states in alcohol dehydrogenase model reactions: rehybridization lags behind H-tunneling
inferred← citeshttps://doi.org/10.1039/c3cp55131hopenalex-snapshot
Proton tunnelling and promoting vibrations during the oxidation of ascorbate by ferricyanide?
inferred← citeshttps://doi.org/10.1039/c4cs00351aopenalex-snapshot
Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently
inferred← citeshttps://doi.org/10.1039/c5cp00614gopenalex-snapshot
Nuclear quantum tunnelling in enzymatic reactions – an enzymologist's perspective
inferred← citeshttps://doi.org/10.1039/c5cp00794aopenalex-snapshot
Protein motions and dynamic effects in enzyme catalysis
inferred← citeshttps://doi.org/10.1039/c5cp02447aopenalex-snapshot
Concepts in bio-molecular spectroscopy: vibrational case studies on metalloenzymes
inferred← citeshttps://doi.org/10.1039/c5sc03666fopenalex-snapshot
Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA)
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