Photosystem II (PSII) is the chlorophyll/protein complex in green plants that catalyzes the oxidation of water to molecular oxygen. We have utilized bacterioferritin (BFR), an iron storage protein found in Escherichia coli, as a protein scaffold to build in PSII cofactors in a simpler in vitro model system. Previously, we have shown that the native heme in BFR can be replaced with the chlorophyll analog zinc-chlorin (ZnCe₆) and that the intrinsic di-iron site can bind two manganese ions. Upon flash excitation of the ZnCe₆ modified BFR, not only is the dinuclear manganese complex oxidized but also a tyrosine residue. There are seven tyrosine residues in each BFR monomeric subunit. We mutated the three tyrosine residues within electron tunnelling distance of the ZnCe₆. Here we present evidence based on electron paramagnetic resonance and fluorescence spectroscopy that one is not oxidized while the other two seem to be oxidized in parallel. Localization of this photoactive tyrosine is the first step in creating a linear electron flow in BFR like in PSII.