LAUSR

Abstract Hydrogenase from the hyperthermophilic bacterium Aquifex aeolicus was immobilized in MgO-templated carbon (MgOC). Two different pore sizes were investigated, large pore size of 150 nm (MgOC150) and smaller pore size of 35 nm (MgOC35). Direct H2 oxidation proceeded in both MgOC150 and MgOC35. Hydrogenase embedded in the carbon material exhibited the expected properties in terms of onset for H2 oxidation and kinetics of formation of the inactive state at high potentials, whatever the size of the pores. Pore size much larger than the size of the enzyme favored the loading of the enzyme, yielding to high catalytic current reported to the capacitance. Pore size closer to the enzyme diameter, as determined by DLS, enhanced the stability of the enzyme at high temperature.