Ordered-Mesoporous-Carbon-Bonded Cobalt Phthalocyanine: A Bioinspired Catalytic System for Controllable Hydrogen Peroxide Activation

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

Metalloporphyrin-based porous polymers prepared via click chemistry for size-selective adsorption of protein

<p>Zinc porphyrin-based porous polymers (PPs-Zn) with different pore sizes were prepared by controlling the reaction condition of click chemistry, and the protein adsorption in PPs-Zn and the catalytic activity of immobilized enzyme were investigated. PPs-Zn-1 with 18 nm and PPS-Zn-2 with 90 nm of pore size were characterized by FTIR, NMR and nitrogen absorption experiments. The amount of adsorbed protein in PPs-Zn-1 was more than that in PPs-Zn-2 for small size proteins, such as lysozyme, lipase and bovine serum albumin (BSA). And for large size proteins including myosin and human fibrinogen (HFg), the amount of adsorbed protein in PPs-Zn-1 was less than that in PPs-Zn-2. The result indicates that the protein adsorption is size-selective in PPs-Zn. Both the protein size and the pore size have a significant effect on the amount of adsorbed protein in the PPs-Zn. Lipase and lysozyme immobilized in PPs-Zn exhibited excellent reuse stability.</p