Phthalocyanines (PC) have long been used for their photophysical properties namely as dye stuffs due to their high molar absorptivities. Due to their colorful nature PC have been the center of research into their photochemistry, this has lead to specific interest in PCs as agents for photo-induced electron transfer. In order to obtain control over these properties the PCs must be isolated in order exclude aggregation of the PCs. Utilize the tools of protein design to construct a scaffold for precise control of PC derivates their properties can be exploited and modular protein designs can be made and inserted into natural or designed protein systems. Reengineering a previously designed maquette protein that binds two heme molecules, we have designed a scaffold that can bind either heme or phthalocyanine derivates. In experiments, we have been able to bind iron phthalocyanine and ruthenium phthalocyanine in the same protein with positional control. This construct has also been used to make mixed species of one heme and one PC in order to demonstrate light-activated charge transfer. The ultimate goal lies in biomaterials which utilize the photochemistry of PCs in solar energy conversion and light-gated ET wires..