Synergistic Catalysis of Enzymes and Biomimetic MOFs: Immobilizing Cyt c on Two-dimensional MOFs to Enhance the Performance of Peroxidase

Metal-organic frameworks(MOFs) have been widely regarded as promising carriers for enzyme immobilization owing to their advantages in improving loading and regulating interaction with enzymes. However, they are still suffering from the problems of slow mass transfer and compromising activity. In this paper, the active two-dimensional(2D) MOF of Cu-TCPP(Fe)[TCPP=tetrakis(4-carboxy-phenyl)porphyrin], which possesses the biomimetic architecture of peroxidase, was adopted to anchor cytochrome(Cyt c) for the enhancement of catalytic activity. The atomic/nanometer thickness and micrometer lateral dimension of 2D MOFs can ensure the full exposure of immobilized enzymes and a shorter diffusion distance for the reactant molecules. Besides, the active carrier can provide synergistic catalysis and activity compensation during the reaction. When tested in the decomposition reaction of H₂O₂, Cyt c/Cu-TCPP(Fe) exhibited nearly twice catalytic activity and an accelerated catalytic rate compared to free Cyt c. [Figure not available: see fulltext.]