The metalloenzyme [FeFe]-hydrogenase is of interest to future biotechnologies targeting the production of "green" hydrogen (H₂ ). We recently developed a simple two-step functionalized procedure to immobilize the [FeFe]-hydrogenase from Clostridium pasteurianum ("CpI") on mesoporous indium tin oxide (ITO) electrodes to achieve elevated H₂ production with high operational stability and current densities of 8 mA cm^-2 . Here, we use a combination of atomic force microscopy (AFM), scanning electron microscopy (SEM) and electrochemical quartz crystal microbalance (EQCM) to understand how mesoporous ITO stabilizes and activates CpI for electroenzymatic H₂ production. Examination of the topography and morphology of the mesoporous ITO surface revealed a hierarchical morphology containing cavities and well-defined nanoparticle agglomerates. Any potential effect of mesoporosity was investigated by comparing the stability and electroenzymatic activity of CpI on mesoporous 'nanoITO' and planar ITO, where we determined that CpI has a higher turnover frequency and adsorbs with greater stability (with respect to electroenzymatic activity over time) to nanoITO surfaces.