Microperoxidase-11 has for the first time been successfully immobilized into a mesoporous metal-organic framework (MOF) consisting of nanoscopic cages and it demonstrates superior enzymatic catalysis performances compared to its mesoporous silica counterpart.

It has been demonstrated for the first time that the heme protein cytochrome c (Cyt c) can enter the interior of a MOF despite the larger molecular dimension of the protein relative to the access pore sizes. Mechanistic studies suggest that the Cyt c molecules must undergo a significant conformational change during translocation into the MOF interior through the relatively small nanopores.

The protein myoglobin has been successfully immobilized into a mesoporous metal-organic framework with hierarchical pore sizes, which demonstrates interesting size-selective biocatalysis as well as superior catalytic activities toward small substrate oxidation compared to its mesoporous silica material counterpart.

Fe3+ complexes of pyridine-containing copolymers were found to be efficient and selective catalysts toward phosphodiester hydrolysis and show significant activity toward oxidative DNA cleavage. The catalysis toward bis(p-nitrophenyl)phosphate (BNPP) hydrolysis exhibits enzyme-like pre-equilibrium kinetics with maximum activities in the range of ca. pH 6-8 and a first-order catalytic proficiency (k cat /k o ) of 4.2ϫ 10 7 -fold at the acidic pH value of 5.3 (i.e., pK a of the coordinated nucleophilic water) and 25°C, entitling this Fe 3+ copolymer an acid phosphodiester catalyst.

Despite the mainly inhomogeneous and unstructured nature of linear polymers, the Cu II complex of a vinylpyridine-acrylamide copolymer exhibits very efficient 2-electron catalysis toward the oxidation of catechol and derivatives to form quinones with and without 80 mM (0.27 %) H 2 O 2 , showing remarkable (0.114-2.67) ϫ 10 5 and (2.83-9.60) ϫ 10 4 -fold rate enhancements, respectively, in terms of first-order rate constant relative to auto-oxidation of the substrates in an aqueous environment under mild conditions. Metal-binding profiles suggest the presence of cooperativity in the catalysis. The oxidation catalysis is inhibited by the di-copper tyrosi-