Hydrogenases as catalysts for fuel cells: Strategies for efficient immobilization at electrode interfaces

Hydrogenases are the key enzymes for hydrogen metabolism in many microorganisms. Due to the high efficiency they develop for H2 oxidation, research in the last five years has aimed towards their use as biocatalysts for H2/O2 biofuel cells to replace platinum-based chemical catalysts. We report in this review the major issues that have been addressed in view of the future development of such a novel biotechnological device. This includes enhancing the stability of either the enzyme itself or its immobilization onto conductive supports, increasing the amount of electrically connected enzymes and, finally, controlling hydrogenase orientation at the electrode surface, and hence the electron transfer process. We specifically focus on a particular [NiFe] membrane-bound hydrogenase purified from the hyperthermophilic and microaerophilic bacterium Aquifex aeolicus. This enzyme resists to O2, CO, and high temperatures making it potentially efficient as a biocatalyst. Recent progress in these domains strengthens the credibility of a viable H2/O2 biofuel cell and opens new avenues for biofuel cell design.

► This review examines hydrogenases as suitable biocatalysts for H2/O2 biofuel cells.
► It focuses on a O2, CO and temperature-resistant hydrogenase from Aquifex aeolicus.
► Electrically connected hydrogenase amount increases on carbon nanotube network.
► Hydrogenase orientation at the interface controls the electron transfer process.
► Hydrogenase insertion into liposomes enhances its stability.