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Halide-free deep eutectic solvents (DESs) derived from natural biological compounds were used to gently catalyze the cycloaddition reaction between CO and epoxides, with a TOF of 645 h. The DFT calculation result was in good agreement with the experiment result, indicating that the ring closure process was the rate-determining step.
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http://dx.doi.org/10.1039/d4cc06282e | DOI Listing |
Chem Commun (Camb)
February 2025
Key Laboratory of Green Chemistry and Technology Ministry of Education, College of Chemistry, Sichuan University, Chengdu 610064, P. R. China.
Halide-free deep eutectic solvents (DESs) derived from natural biological compounds were used to gently catalyze the cycloaddition reaction between CO and epoxides, with a TOF of 645 h. The DFT calculation result was in good agreement with the experiment result, indicating that the ring closure process was the rate-determining step.
View Article and Find Full Text PDFMaterials (Basel)
February 2024
Materials Innovation Centre, School of Engineering, University of Leicester, Leicester LE1 7RH, UK.
Zinc electrodeposition serves as a crucial electrochemical process widely employed in various industries, particularly in automotive manufacturing, owing to its cost effectiveness compared to traditional methods. However, traditional zinc electrodeposition using aqueous solutions faces challenges related to toxicity and hydrogen gas generation. Non-aqueous electrolytes such as ionic liquids (ILs) and deep eutectic solvents (DESs) have gained attention, with choline-chloride-based DESs showing promise despite raising environmental concerns.
View Article and Find Full Text PDFBiophys J
July 2003
Graduate Group in Biophysics, University of California, Berkeley, California 94720, USA.
We report the crystal structure of a bromide-bound form of the D85S mutant of bacteriorhodopsin, bR(D85S), a protein that uses light energy rather than ATP to pump halide ions across the cell membrane. Comparison of the structure of the halide-bound and halide-free states reveals that both displacements of individual side-chain positions and concerted helical movements occur on the extracellular side of the protein. Analysis of these structural changes reveals how this ion pump first facilitates ion uptake deep within the cell membrane and then prevents the backward escape of ions later in the pumping cycle.
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