ArticleProceedings of the National Academy of Sciences of the United States of America2011
Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomerase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 51 citations in OpenAlex.
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- Photosynthetic reaction center variants made via genetic code expansion show Tyr at M210 tunes the initial electron transfer mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Integrating single-cobalt-site and electric field of boron nitride in dechlorination electrocatalysts by bioinspired design.Nature communications · 2021Article
- Comment on "Transient Conformational Changes of Sensory Rhodopsin II Investigated by Vibrational Stark Effect Probes".The journal of physical chemistry. B · 2017Article
- Electric Fields and Enzyme Catalysis.Annual review of biochemistry · 2017Review
- BIOPHYSICS. Response to Comments on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".Science (New York, N.Y.) · 2015Article
- Site-specific infrared probes of proteins.Annual review of physical chemistry · 2015Review
- Perspectives on electrostatics and conformational motions in enzyme catalysis.Accounts of chemical research · 2015Review
- 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
- Probing the electrostatics of active site microenvironments along the catalytic cycle for Escherichia coli dihydrofolate reductase.Journal of the American Chemical Society · 2014Article
- Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis.The journal of physical chemistry. B · 2014Article
- Calculations of the electric fields in liquid solutions.The journal of physical chemistry. B · 2013Article
- Measuring electrostatic fields in both hydrogen-bonding and non-hydrogen-bonding environments using carbonyl vibrational probes.Journal of the American Chemical Society · 2013Article
- Quantitative dissection of hydrogen bond-mediated proton transfer in the ketosteroid isomerase active site.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Solvatochromism and the solvation structure of benzophenone.The Journal of chemical physics · 2013Article
- Fundamental challenges in mechanistic enzymology: progress toward understanding the rate enhancements of enzymes.Biochemistry · 2013Review
- Calculation of vibrational shifts of nitrile probes in the active site of ketosteroid isomerase upon ligand binding.Journal of the American Chemical Society · 2013Article
- A quantitative measure of electrostatic perturbation in holo and apo enzymes induced by structural changes.PloS one · 2013Article
- Validation of response function construction and probing heterogeneous protein hydration by intrinsic tryptophan.The journal of physical chemistry. B · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Understanding how electric fields and their fluctuations in the active site of enzymes affect efficient catalysis represents a critical objective of biochemical research. We have directly measured the dynamics of the electric field in the active site of a highly proficient enzyme, Δ(5)-3-ketosteroid isomerase (KSI), in response to a sudden electrostatic perturbation that simulates the charge displacement that occurs along the KSI catalytic reaction coordinate. Photoexcitation of a fluorescent analog (coumarin 183) of the reaction intermediate mimics the change in charge distribution that occurs between the reactant and intermediate state in the steroid substrate of KSI. We measured the electrostatic response and angular dynamics of four probe dipoles in the enzyme active site by monitoring the time-resolved changes in the vibrational absorbance (IR) spectrum of a spectator thiocyanate moiety (a quantitative sensor of changes in electric field) placed at four different locations in and around the active site, using polarization-dependent transient vibrational Stark spectroscopy. The four different dipoles in the active site remain immobile and do not align to the changes in the substrate electric field. These results indicate that the active site of KSI is preorganized with respect to functionally relevant changes in electric fields.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.