Topological transformation of microbial proteins into iron single-atom sites for selective hydrogen peroxide electrosynthesis

Nat Commun. 2024 Dec 30;15(1):10758. doi: 10.1038/s41467-024-55041-z.

Abstract

The emergence of single-atom catalysts offers exciting prospects for the green production of hydrogen peroxide; however, their optimal local structure and the underlying structure-activity relationships remain unclear. Here we show trace Fe, up to 278 mg/kg and derived from microbial protein, serve as precursors to synthesize a variety of Fe single-atom catalysts containing FeN5-xOx (1 ≤ x ≤ 4) moieties through controlled pyrolysis. These moieties resemble the structural features of nonheme Fe-dependent enzymes while being effectively confined on a microbe-derived, electrically conductive carbon support, enabling high-current density electrolysis. A comparative analysis involving catalysts derived from eleven representative microbes reveals that the presence of 0.05 wt% Fe single-atom sites leads to a significant 26% increase in hydrogen peroxide selectivity. Remarkably, the optimal catalyst featuring FeN3O2 sites demonstrates a selectivity of up to 93.7% and generates hydrogen peroxide in a flow cell at an impressive rate of 29.6 mol g-1 h-1 at 200 mA cm-2. This work achieves structural fine-tuning of metal single-atom sites at the trace level and provides topological insights into single-atom catalyst design to achieve cost-efficient hydrogen peroxide production.

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Catalysis
  • Electrolysis
  • Hydrogen Peroxide* / chemistry
  • Hydrogen Peroxide* / metabolism
  • Iron* / chemistry
  • Iron* / metabolism
  • Oxidation-Reduction

Substances

  • Hydrogen Peroxide
  • Iron
  • Bacterial Proteins