Catalytic Wiring of Enzymatic Cascades Using ROS-Flux-Regulated Biodegradable Borophene

Two-dimensional (2D) borophene, a single-atom-thick allotrope of boron, exhibits exceptional conductivity, anisotropy, and chemical reactivity, yet very little is known about its electrochemical properties. Here, we delineate its enzymatic and electrochemical behavior under biologically relevant redox conditions. Spectroscopic and microscopic studies reveal concentration-dependent degradation of borophene by hydrogen peroxide (H₂O₂), yielding boronic acids, confirmed by a curcumin-rosocyanine assay. Enzymatic cascades employing glucose oxidase and horseradish peroxidase establish borophene as both an electrocatalyst and a chemically responsive transducer, generating dual colorimetric and electrochemical outputs. Electroanalytical measurements (cyclic voltammetry, chronoamperometry, and differential pulse voltammetry) show that borophene efficiently wires peroxidase reactions by sensitizing H₂O₂ detection through borophene-HRP interfaces. In contrast, glucose sensing displays diminished currents due to reactive oxygen species-mediated passivation. These results position borophene as a unique platform for catalytic wiring of enzyme cascades in which ROS flux dynamically regulates signal output, enabling transient, self-reporting biosensors and motivating stabilization strategies for long-term bioelectronic integration.