To leverage the versatile catalytic activity of FePP catalysts, we aimed to integrate FePP into Sav (Streptavidin). Considering the dimer-of-dimers nature of Sav, we envisioned endowing the FePP moiety with two biotin anchors to firmly secure the cofactor within the biotin-binding vestibule. However, attempts to synthesize unsymmetrical porphyrins often resulted in low yields. To address these synthetic challenges, we introduced two biotins at opposing meso-positions of the porphyrin, using an anionic, non-coordinating spacer: L-cysteic acid. We speculated that length of the amino acid spacer would favour the intramolecular coordination of the Biot2 ─ FePP • Sav cofactor, minimizing the formation of crosslinked streptavidin oligomers resulting from intermolecular coordination of the cofactor.