Simple Design of an Enzyme-Inspired Supported Catalyst Based on a Catalytic Triad
| Autor: | Craig J. Hawker, Megan L. O'Mara, Ezat Khoshdel, Ashley Davalos, Aravindhan Ganesan, Mitchell D. Nothling, Zeyun Xiao, Luke A. Connal, Michelle L. Coote, Michael R. Gotrik, Eric D. Pressly, Karmen Condic-Jurkic |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
chemistry.chemical_classification
010405 organic chemistry General Chemical Engineering Biochemistry (medical) General Chemistry 010402 general chemistry 01 natural sciences Biochemistry 0104 chemical sciences Merrifield resin Catalysis chemistry.chemical_compound Enzyme chemistry Dendrimer Catalytic triad Click chemistry Materials Chemistry Imidazole Organic chemistry Environmental Chemistry Carboxylate |
| Zdroj: | Chem. 2:893-894 |
| ISSN: | 2451-9294 |
| DOI: | 10.1016/j.chempr.2017.05.015 |
| Popis: | Summary Enzyme active sites afford an intricate interplay of functional groups to mediate complex organic and inorganic reactions. Many hydrolytic enzymes use a catalytic triad comprising three different functional residues—(Ser(-OH), Hist(-imidazole), Asp(-CO 2 H))—that catalyze the hydrolysis of numerous unique substrates. Inspired by this design, we have developed a simple one-step synthesis for preparing a new supported catalytic system in which the three reactive groups of the catalytic triad (alcohol, imidazole, and carboxylate) are incorporated into a single functional unit. These artificial active sites can be coupled to a solid-phase support (Merrifield resin) by copper(I)-catalyzed azide-alkyne cycloaddition "click chemistry," and their effectiveness as esterolysis catalysts was demonstrated. Furthermore, tuning the local hydrophobicity of the resin particles with an approach analogous to the native enzyme hydrophobic pocket increased the catalytic efficiency. Quantum mechanics and molecular dynamics computational modeling were used to probe the catalytic effect and suggested a concerted two-step mechanism and hydrophobic nanoenvironment similar to that of hydrolytic enzymes. |
| Databáze: | OpenAIRE |
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