ArticleJournal of the American Chemical Society2010
Solvation response along the reaction coordinate in the active site of ketosteroid isomerase.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 36 citations in OpenAlex.
- Engineering drug-protein kinetics via intrinsic quantum Stark fields in binding motifs.Journal of molecular modeling · 2025Article
- Quantified electrostatic preorganization in enzymes using the geometry of the electron charge density.Chemical science · 2017Article
- Extreme electric fields power catalysis in the active site of ketosteroid isomerase.Science (New York, N.Y.) · 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
- 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
- Catalytic efficiency of enzymes: a theoretical analysis.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
- Site-specific measurement of water dynamics in the substrate pocket of ketosteroid isomerase using time-resolved vibrational spectroscopy.The journal of physical chemistry. B · 2012Article
- Direct measurement of the protein response to an electrostatic perturbation that mimics the catalytic cycle in ketosteroid isomerase.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A light-activated reaction analog has been developed to mimic the catalytic reaction cycle of Delta(5)-3-ketosteroid isomerase to probe the functionally relevant protein solvation response to the catalytic charge transfer. Delta(5)-3-ketosteroid isomerase from Pseudomonas putida catalyzes a C-H bond cleavage and formation through an enolate intermediate. Conversion of the ketone substrate to the enolate intermediate is simulated by a photoacid bound to the active site oxyanion hole. In the ground state, the photoacid electrostatically resembles the enolate intermediate while the low pK(a) excited state resembles the ketone starting material. Time-resolved fluorescence experiments with photoacids coumarin 183 and equilenin show the active site of Delta(5)-3-ketosteroid isomerase to be largely unperturbed by the light-activated reaction. The small solvation response for the photoacid at the active site as compared with a simple solvent suggests the active site does not significantly change its electrostatic environment during the catalytic cycle. Instead, the reaction takes place in an electrostatically preorganized environment.
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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.