Reaction of the hydroxyl group of serine-221 of subtilisin with phenylmethanesulfonylfluoride followed by nucleophilic substitution with sodium hydrogen telluride, a semisynthetic telluroprotein, tellurosubtilisin, was prepared. Tellurosubtilisin, which displays high substrate specificity for aromatic thiols, exhibits remarkable peroxidase activity and catalyzes the reduction of hydrogen peroxide by 3-carboxy-4-nitrobenzenethiol 20 000 times more efficiently than diphenyl diselenide.

An artificial nanozyme model was developed by the supramolecular complexation of a b-cyclodextrinmodified gold nanoparticle and metal catalytic centers. The cyclodextrin-based monolayer was first constructed on the surface of gold nanoparticle by using the thiol modified cyclodextrin, subsequently the cyclodextrin-modified gold nanoparticle was utilized as a backbone to install metal catalytic centers by supramolecular assembly of the copper complex of triethylnetetramine-adamantane and b-cyclodextrin receptors immobilized on the surface of gold nanospheres via hydrophobic interaction. The catalytic behaviors of b-cyclodextrin-modified gold nanoparticles with adjacent multi-metal catalytic centers were investigated as an esterase mimic. Strong hydrolase activities for catalyzing the cleavage of an active ester 4,4 0 -dinitrodiphenyl carbonate (DNDPC) were observed. A detailed kinetic study on nanozyme-catalyzed hydrolysis of ester DNDPC has been described.

It has long been known that tellurium compounds are rather toxic to living organisms, and tellurium has not been found in natural biomacromolecules to date. The principles of telluride toxicity in biological processes are still controversial partly because of the lack of information on the biochemical features of tellurium. In this contribution, we report our finding for the first time that telluroxides exhibit hydrolysis capacity. For instance, 6,6'-telluroxy-bis(6-deoxy-beta-cyclodextrin) acts as a hydrolase mimic and shows a significant rate acceleration of 106,000 for the hydrolysis of 4,4'-dinitrodiphenyl carbonate.

No abstract

Water-soluble Au nanocrystal (NC) micelles with an inserted catalytic Cu(II) center that act as excellent nanoenzyme models for imitating ribonuclease were constructed by supramolecular self-assembly. The dodecane-1-thiol-based Au NC was constructed first, and subsequently the cationic surfactant hexadecyltrimethylammonium bromide and the catalytic ligand (N1,N1-bis(2-aminoethyl)-N2-dodecylethane-1,2-diamine) copper(II) were installed on the surface of the Au NC via hydrophobic interaction. The catalytic capability of the Au NC micelles designed was estimated by the cleavage of a typical RNA analogue, 2-hydroxypropyl p-nitrophenyl phosphate (HPNP). The study of the catalytic behavior of Au NC micelle catalysis showed that the Au NC micelles exhibited dramatic ribonuclease-like activity: a high rate acceleration of k(cat)/k(uncat) = 1.10 x 10(5) for the cleavage of HPNP in comparison with the spontaneous cleavage of HPNP (k(uncat)) was observed. The catalytic capability for HPNP cleavage by these functionalized Au NC micelles can be compared with that of covalent Au nanoparticles reported previously as nanozymes under comparable conditions. A detailed investigation of enzymatic kinetics was carried out and a possible mechanism was suggested.