ArticleMethods in enzymology2015
Resolution and Characterization of Chemical Steps in Enzyme Catalytic Sequences by Using Low-Temperature and Time-Resolved, Full-Spectrum EPR Spectroscopy in Fluid Cryosolvent and Frozen Solution Systems.
Article in Methods in enzymology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 17 citations in OpenAlex.
- Protein structure and coupled solvent dynamics in α-synuclein fibrils under controlled confinement.Biophysical journal · 2026Article
- Select Configurational Dynamics in Ethanolamine Ammonia-Lyase Radical Enzyme Catalysis.ACS physical chemistry Au · 2025Article
- Physical and Mechanical Properties of Monomeric Alpha-Synuclein Provide Leads to Molecular Function.The journal of physical chemistry. B · 2025Article
- Oligomeric and Fibrillar α-Synuclein Display Persistent Dynamics and Compressibility under Controlled Confinement.ACS chemical neuroscience · 2023Article
- Native and nonnative reactions in ethanolamine ammonia-lyase are actuated by different dynamics.Biophysical journal · 2023Article
- Reactivity Tracking of an Enzyme Progress Coordinate.The journal of physical chemistry letters · 2023Article
- Confinement dependence of protein-associated solvent dynamics around different classes of proteins, from the EPR spin probe perspective.Physical chemistry chemical physics : PCCP · 2022Article
- Resolution and characterization of confinement- and temperature-dependent dynamics in solvent phases that surround proteins in frozen aqueous solution by using spin-probe EPR spectroscopy.Methods in enzymology · 2022Article
- Resolution and characterization of contributions of select protein and coupled solvent configurational fluctuations to radical rearrangement catalysis in coenzyme BMethods in enzymology · 2022Article
- Coupling of ethanolamine ammonia-lyase protein and solvent dynamics characterized by the temperature-dependence of EPR spin probe mobility and dielectric permittivity.The Journal of chemical physics · 2021Article
- Deuterium Kinetic Isotope Effects Resolve Low-Temperature Substrate Radical Reaction Pathways and Steps in BBiochemistry · 2019Article
- Control of Solvent Dynamics around the BThe journal of physical chemistry. B · 2019Article
- Protein Configurational States Guide Radical Rearrangement Catalysis in Ethanolamine Ammonia-Lyase.Biophysical journal · 2018Article
- Density and electron density of aqueous cryoprotectant solutions at cryogenic temperatures for optimized cryoprotection and diffraction contrast.Acta crystallographica. Section D, Structural biology · 2018Article
- Electron spin-labelling of the EutC subunit in BFree radical research · 2018Article
- Mesodomain and Protein-Associated Solvent Phases with Temperature-Tunable (200-265 K) Dynamics Surround Ethanolamine Ammonia-Lyase in Globally Polycrystalline Aqueous Solution Containing Dimethyl Sulfoxide.The journal of physical chemistry. B · 2017Article
- Two Dynamical Regimes of the Substrate Radical Rearrangement Reaction in BBiochemistry · 2017Article
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4 authors at 1 institution in 1 country.
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Abstract
Approaches to the resolution and characterization of individual chemical steps in enzyme catalytic sequences, by using temperatures in the cryogenic range of 190-250 K, and kinetics measured by time-resolved, full-spectrum electron paramagnetic resonance spectroscopy in fluid cryosolvent and frozen solution systems, are described. The preparation and performance of the adenosylcobalamin-dependent ethanolamine ammonia-lyase enzyme from Salmonella typhimurium in the two systems exemplifies the biochemical and spectroscopic methods. General advantages of low-temperature studies are (1) slowing of reaction steps, so that measurements can be made by using straightforward T-step kinetic methods and commercial instrumentation, (2) resolution of individual reaction steps, so that first-order kinetic analysis can be applied, and (3) accumulation of intermediates that are not detectable at room temperatures. The broad temperature range from room temperature to 190 K encompasses three regimes: (1) temperature-independent mean free energy surface (corresponding to native behavior); (2) the narrow temperature region of a glass-like transition in the protein, over which the free energy surface changes, revealing dependence of the native reaction on collective protein/solvent motions; and (3) the temperature range below the glass transition region, for which persistent reaction corresponds to nonnative, alternative reaction pathways, in the vicinity of the native configurational envelope. Representative outcomes of low-temperature kinetics studies are portrayed on Eyring and free energy surface (landscape) plots, and guidelines for interpretations are presented.
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