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Heme biomolecule as redox mediator and oxygen shuttle for efficient charging of lithium-oxygen batteries.


ABSTRACT: One of the greatest challenges with lithium-oxygen batteries involves identifying catalysts that facilitate the growth and evolution of cathode species on an oxygen electrode. Heterogeneous solid catalysts cannot adequately address the problematic overpotentials when the surfaces become passivated. However, there exists a class of biomolecules which have been designed by nature to guide complex solution-based oxygen chemistries. Here, we show that the heme molecule, a common porphyrin cofactor in blood, can function as a soluble redox catalyst and oxygen shuttle for efficient oxygen evolution in non-aqueous Li-O2 batteries. The heme's oxygen binding capability facilitates battery recharge by accepting and releasing dissociated oxygen species while benefiting charge transfer with the cathode. We reveal the chemical change of heme redox molecules where synergy exists with the electrolyte species. This study brings focus to the rational design of solution-based catalysts and suggests a sustainable cross-link between biomolecules and advanced energy storage.

SUBMITTER: Ryu WH 

PROVIDER: S-EPMC5075788 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature

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Heme biomolecule as redox mediator and oxygen shuttle for efficient charging of lithium-oxygen batteries.

Ryu Won-Hee WH   Gittleson Forrest S FS   Thomsen Julianne M JM   Li Jinyang J   Schwab Mark J MJ   Brudvig Gary W GW   Taylor André D AD  

Nature communications 20161019


One of the greatest challenges with lithium-oxygen batteries involves identifying catalysts that facilitate the growth and evolution of cathode species on an oxygen electrode. Heterogeneous solid catalysts cannot adequately address the problematic overpotentials when the surfaces become passivated. However, there exists a class of biomolecules which have been designed by nature to guide complex solution-based oxygen chemistries. Here, we show that the heme molecule, a common porphyrin cofactor i  ...[more]

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