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Area of Science:

  • * Electrochemistry
  • * Computational Chemistry
  • * Enzyme Engineering

Background:

  • * Biocathodes utilize enzymes for electrochemical reactions.
  • * Bilirubin oxidase (BOx) is a key enzyme for biocathode development.
  • * Understanding enzyme-electrode interfaces is crucial for improving biocathode efficiency.

Purpose of the Study:

  • * To investigate the role of bilirubin in enhancing biocathode performance using computational and experimental methods.
  • * To study the interface interactions between bilirubin oxidase and a modified electrode surface.
  • * To elucidate the mechanism by which bilirubin improves electron transfer.

Main Methods:

  • * Density functional theory (DFT) calculations.
  • * Molecular docking simulations.
  • * Electrochemical characterization using potentiostatic measurements.
  • * Electrode surface modification via bilirubin adsorption.

Main Results:

  • * Bilirubin adsorption significantly improved cathode operation, as evidenced by increased current densities.
  • * Computational analysis revealed bilirubin acts as a geometric and electronic extension of the graphene support.
  • * Bilirubin facilitates interfacial electron transfer by optimizing BOx orientation and reducing the distance to the T1 Cu atom.

Conclusions:

  • * Bilirubin acts as a crucial mediator at the enzyme-electrode interface.
  • * The combination of DFT and docking simulations is effective for studying biocathode interfaces.
  • * Electrode modification with bilirubin offers a promising strategy for enhanced biocathode performance.