Construction of a Novel Guest Biomimetic Glutathione Peroxidase with Solvent-Dependent Catalytic Behavior by Incorporating the Active Center into Adamantyl Molecule~1

摘要

A novel guest biomimetic glutathione peroxidase(3,3'-tellurobis(propane-3,1-diyl) diadamantan- ecarboxylate, denoted as ADA-Te-ADA) was synthesized. ADA-Te-ADA functioned to overcome the disad- vantages in the construction of building block for giant supramolecular biomimetic enzyme. To reveal the cat- alytic property of hydrophobic ADA-Te-ADA, the catalytic mechanism was investigated using PBS (phos- phate buffer (pH = 7.0, 50 mM))/methanol solvent mixture as assay solution. It indicated that ADA-Te-ADA exhibited typical enzyme catalytic behavior by saturation kinetics measurement. Importantly, ADA-Te-ADA exhibited the typical solvent-dependent catalytic behavior. And the highest catalytic rate 4.29 μM × min~(-1) was obtained when the volume ratio of PBS: methanol was 5: 5. Especially, the catalytic rates obtained based on various substrates proved that ADA-Te-ADA slightly displayed special substrate selectivity, which was the ideal catalytic characterization of building block for giant supramolecular biomimetic enzyme. The success- fully synthesis of ADA-Te-ADA might highlight for the understanding of the catalytic mechanism of hydro- phobic guest biomimetic glutathione peroxidase. And it also might provide the basement for the construction of giant supramolecular biomimetic enzyme.