Abstract
The chemistry of enzymes presents a key to understanding the catalysis in the world. In the pursuit of controllable catalytic oxidation, researchers make extensive efforts to discover and develop functional materials that exhibit various properties intrinsic to enzymes. Here we describe a bioinspired catalytic system using ordered-mesoporous-carbon (OMC)-bonded cobalt tetraaminophthalocyanine (CoTAPc-OMC) as a catalyst that could mimic the space environment and reactive processes of metalloporphyrin-based heme enzymes and employing linear dodecylbenzenesulfonate as the fifth ligands to control the activation of H2O2 toward the peroxidase-like oxidation. The generation of nonselective free hydroxyl radicals was obviously inhibited. In addition, functional modification of OMC has been achieved by a moderate method, which can reduce excessive damage to the structure of OMC. Because of its favorable and tunable pore texture, CoTAPc-OMC provides a suitable interface and environment for the accessibility and oxidation of C.I. Acid Red 1, the model compound, and exhibits significantly enhanced catalytic activity and sufficient stability for H2O2 activation. The high-valent cobalt oxo intermediates with high oxidizing ability have been predicted as the acceptable active species, which have been corroborated by the results from the semiempirical quantum-chemical PM6 calculations.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.