ArticleThe journal of physical chemistry. B2012
Site-specific measurement of water dynamics in the substrate pocket of ketosteroid isomerase using time-resolved vibrational spectroscopy.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 21 citations in OpenAlex.
- Transparent window 2D IR spectroscopy of proteins.The Journal of chemical physics · 2021Review
- Distinguishing Potassium Channel Resting State Conformations in Live Cells with Environment-Sensitive Fluorescence.ACS chemical neuroscience · 2020Article
- Optical mapping of biological water in single live cells by stimulated Raman excited fluorescence microscopy.Nature communications · 2019Article
- Protein Solvent Shell Structure Provides Rapid Analysis of Hydration Dynamics.Journal of chemical information and modeling · 2019Article
- Entropy connects water structure and dynamics in protein hydration layer.Physical chemistry chemical physics : PCCP · 2018Article
- Probing the Effects of Gating on the Ion Occupancy of the KJournal of the American Chemical Society · 2017Article
- SAXS/SANS on Supercharged Proteins Reveals Residue-Specific Modifications of the Hydration Shell.Biophysical journal · 2016Article
- BIOPHYSICS. Response to Comments on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".Science (New York, N.Y.) · 2015Article
- Metal-ion effects on the polarization of metal-bound water and infrared vibrational modes of the coordinated metal center of Mycobacterium tuberculosis pyrazinamidase via quantum mechanical calculations.The journal of physical chemistry. B · 2014Article
- Implementing electrostatic polarization cannot fill the gap between experimental and theoretical measurements for the ultrafast fluorescence decay of myoglobin.Journal of molecular modeling · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Little is known about the reorganization capacity of water molecules at the active sites of enzymes and how this couples to the catalytic reaction. Here, we study the dynamics of water molecules at the active site of a highly proficient enzyme, Δ(5)-3-ketosteroid isomerase (KSI), during a light-activated mimic of its catalytic cycle. Photoexcitation of a nitrile-containing photoacid, coumarin183 (C183), mimics the change in charge density that occurs at the active site of KSI during the first step of the catalytic reaction. The nitrile of C183 is exposed to water when bound to the KSI active site, and we used time-resolved vibrational spectroscopy as a site-specific probe to study the solvation dynamics of water molecules in the vicinity of the nitrile. We observed that water molecules at the active site of KSI are highly rigid, during the light-activated catalytic cycle, compared to the solvation dynamics observed in bulk water. On the basis of this result, we hypothesize that rigid water dipoles at the active site might help in the maintenance of the preorganized electrostatic environment required for efficient catalysis. The results also demonstrate the utility of nitrile probes in measuring the dynamics of local (H-bonded) water molecules in contrast to the commonly used fluorescence methods which measure the average behavior of primary and subsequent spheres of solvation.
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