Rather than focusing on the structural details of a specific natural protein, we are designing general protein structural scaffolds (''maquettes'') to accommodate a variety of functions. Here we will present transmembrane electron transfer via AP6, an amphiphilic tetra-helical maquette that binds up to 6 hemes. We demonstrate that AP6 self-assembles with phospholipids into vesicles. Our stop flow experiments confirm that the AP6 maquette significantly increases the electron transfer rates between oxidizing interior and an external redox mediator dye, as shown below.