Natural photosynthesis involves the conversion of light into chemical energy through a series of electron transfer reactions within membrane-bound pigment/protein complexes. In the unique Photosystem II complex these electron transfer events result in the oxidation of water to molecular oxygen and hydrogen ions. Production of an in-vitro model of photosystem II will help in the elucidation of the water splitting mechanism. We have developed an artificial light-activated, metal-binding protein, using the naturally occurring bacterioferritin protein (cytochrome b1 or BFR) from E. coli. This protein is not light-active but has many design features which can be utilized to engineer light-driven electron transport. In particular each BFR subunit is a four helix bundle containing a di-iron metal binding site while two identical subunits dimerise to form a hydrophobic heme-binding pocket. The heme group can be easily removed and replaced with a photoactive zinc-chlorin molecule and the iron at the di-metal binding site can be replaced with two divalent manganese ions. Using this modified BFR protein and EPR measurements we have been able to show that the manganese is bound in a redox active form and that upon illumination of the engineered pigment protein complex, the metal centre is oxidised.