The dynamic kinetic resolution of β-aryl α-keto esters has been accomplished using a newly designed (arene)RuCl(monosulfonamide) transfer hydrogenation catalyst. This dynamic process generates three contiguous stereocenters with remarkable diastereoselectivity through a reduction/lactonization sequence. The resulting enantioenriched, densely functionalized γ-butyrolactones are of high synthetic utility, as highlighted by several secondary derivatizations.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3342478 | PMC |
http://dx.doi.org/10.1021/ja3027136 | DOI Listing |
Anal Chem
January 2025
School of Molecular and Cellular Biology and Astbury Centre, University of Leeds, Leeds LS2 9JT, U.K.
Hydrogen/deuterium exchange mass spectrometry (HDX-MS) is a powerful technique to interrogate protein structure and dynamics. With the ability to study almost any protein without a size limit, including intrinsically disordered ones, HDX-MS has shown fast growing importance as a complement to structural elucidation techniques. Current experiments compare two or more related conditions (sequences, interaction partners, excipients, conformational states, etc.
View Article and Find Full Text PDFJ Phys Chem A
January 2025
Department of Chemistry and Chemical Biology, Center for Computational Chemistry, University of New Mexico, Albuquerque, New Mexico 87131, United States.
The kinetics of electronically inelastic quenching of O(Δ) and O(Σ) by collisions with O(P) have been investigated using mixed quantum-classical trajectories governed by adiabatic potential energy surfaces and state couplings generated from a recently developed diabatic potential energy matrix (DPEM) for the 14 lowest-energy A' states of O. Using the coherent switching with decay of mixing (CSDM) method, dynamics calculations were performed both with 14 coupled electronic states and with 8 coupled electronical states, and similar results were obtained. The calculated thermal quenching rate coefficients are generally small, but they increase with temperature.
View Article and Find Full Text PDFEvolution
January 2025
Department of Biological Sciences, Duquesne University, Pittsburgh, PA, 15282, United States.
Male reproductive proteins frequently evolve rapidly in animals, potentially due to adaptive evolution driven by sperm competition, polyspermy avoidance, or pathogen defense. Alternatively, elevated rates of protein change may be due to relaxed constraint. The prostate-specific protease KLK3 has experienced dynamic evolution since its origin stemming from a gene duplication in the ancestor of all Old World primates, with instances of rapid evolution, stasis, and pseudogenization.
View Article and Find Full Text PDFChem Sci
January 2025
Institute of Functional Nano & Soft Materials (FUNSOM), Soochow University Suzhou Jiangsu 215123 China
Understanding the oxygen reduction reaction (ORR) mechanism and accurately characterizing the reaction interface are essential for improving fuel cell efficiency. We developed an active learning framework combining machine learning force fields and enhanced sampling to explore the dynamics and kinetics of the ORR on Fe-N/C using a fully explicit solvent model. Different possible reaction paths have been explored and the O adsorption process is confirmed as the rate-determining step of the ORR at the Fe-N/C-water interface, which needs to overcome a free energy barrier of 0.
View Article and Find Full Text PDFChem Sci
January 2025
Department of Chemical and Biological Physics, Weizmann Institute of Science Rehovot 761001 Israel
Proteins often harness extensive motions of domains and subunits to promote their function. Deciphering how these movements impact activity is key for understanding life's molecular machinery. The enzyme adenylate kinase is an intriguing example for this relationship; it ensures efficient catalysis by large-scale domain motions that lead to the enclosure of the bound substrates ATP and AMP.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!