Spatial Confinement in Structural Biomimetic Catalysts: Enhancing Sulfur-Chain Homolysis and Enzyme-like Activity for High-Performance Lithium-Sulfur Batteries.
basic_science · Level V
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- Record sourced from PubMed, PMID 40814190.
- Also identified by DOI 10.1021/acsnano.5c11892.
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Abstract
Our study addresses the critical challenges of sluggish sulfur reaction kinetics and severe lithium polysulfide shuttling in high-energy-density lithium-sulfur batteries under high sulfur loading and lean electrolyte conditions. Inspired by the structure of cytochrome c oxidase, we designed an enzyme-mimetic Fe-TCPP@Cu-BTC catalyst with spatial confinement effects. Its spatially confined configuration induces the homolytic cleavage of Li<sub>2</sub>S<sub>6</sub> to LiS<sub>3</sub> and accelerates their subsequent conversion to Li<sub>2</sub>S. The enzyme-like properties were further evaluated using Michaelis-Menten kinetics, confirming that the homolytic reaction can increase the sulfur conversion rate by nearly 2 orders of magnitude.