Redox-active nanoscale materials such as porphyrin binding proteins are of immense interest because of their potential use as catalysts in light-energy harvesting processes or as bioelectronic devices. To realize this potential, we have designed simple, robust peptides (maquettes) that assemble into four-helix bundles. The maquettes presented here possess overall amphiphilic character that enables their complex multi-component assembly in detergents, phospholipids vesicles or at air-liquid interfaces. To enable electron transfer within the protein and subsequently across a membrane, we have incorporated multiple binding sites for redox-active cofactors. We have tested how the position of the binding site with respect to the membrane affects the assembly, affinity, and redox properties. Results reported here include AP maquettes with up to 6 binding sites for protoporphyrins.