Rational design of redox active metal organic frameworks for mediated electron transfer of enzymes

The efficient immobilization of redox mediators remains a major challenge in the design of mediated enzyme electrode platforms. In addition to stability, the ability of the redox-active material to mediate electron transfer from the active-site buried enzymes, such as flavin adenine dinucleotide-dependent glucose dehydrogenase (FADGDH) and lactate oxidase (LOx), is also crucial. Conventional immobilization techniques can be synthetically challenging, and immobilized mediators often exhibit limited durability, particularly in continuous operation. Here, we design a novel redox-active cobalt-based metal-organic framework (raMOF) obtained <i>via</i> the partial ligand substitution of 2-methylimidazole (MeIm) with a 1,2-naphthoquinone-4-sulfonate (NQSO) redox probe, as a promising platform for high-performance enzyme electrodes. This nanostructured raMOF, combined with multi-walled carbon nanotubes (CNTs), provided a high current density of up to 2.06 mA cm^-2 during enzymatic reactions and maintained remarkable operational stability, retaining 100% of its current over 54 hours. This stability far exceeded that of adsorbed NQSO on CNTs, which experienced a complete loss of the initial current, highlighting the significant advantage of the raMOF-based platform for high-performance enzyme electrodes.