The critical importance of understanding the local chemical environment of highly active confined enzymes in porous electrodes has been experimentally demonstrated. An independent FEM was also applied to predict the experimental currents, thus verifying the model and allowing the simulation and understanding of local concentration changes, an experimentally challenging feat in these complex multicomponent enzyme systems on porous electrodes. For the HER and the CO2RR, the local pH was shown to increase around 2 pH units due to enzyme catalysis in a confined environment. Dramatic differences in activity were achieved without inhibitively large buffer concentrations, but instead through careful buffer selection and manipulation of the electrolyte pH. In mesoporous electrodes, a 9-fold increase in the HER current density from -0.5 mA cm -2 to -4.8 mA cm -2 produced 50 ± 3 μmol cm -2 h -1 of H2 and a 2-fold current density increase for CO2 reduction, produced 21 ± 0.1 μmol cm -2 h -1 of formate. Finally, in an alternative architecture of inverse opal electrodes, even greater current densities were achieved through the combination of increased mass transport due to macroporous structuring, higher loading and more reductive potentials with an optimised electrolyte. For the HER current densities of -8.0 mA cm -2 produced 80 μmol cm -2 h -1 of H2 with a FE of 92% and for the CO2RR current densities of -3.6 mA cm -2 produced 55 ± 4.3 μmol cm -2 h -1 of formate, over 10 hours giving a total formate production of 0.55 ± 0.043 mmol cm -2 with a FE of (96 ± 8.7)%. These figures demonstrate a 3-fold increase for the HER and an 18-fold increase for the CO2RR on analogous reported electrochemical systems in which the local environment was not considered. Through this work we have shown the ability to use experimental data and computational methods in tandem to analyze and optimise biological-artificial hybrid electrodes.