One interesting and versatile class of metalloproteins is heme proteins, which are among the most well-studied and have played a key role in shaping our understanding of protein structure and function. By fully understanding how metalloproteins function, we can apply this knowledge to design functional metalloproteins from scratch that bind non-biological metallocofactors, such as corroles, which possess unique redox properties and enhanced reactivity. This unique feature offers a distinct advantage in designing metalloproteins to access highly oxidizing species. By designing a protein backbone to stabilize and bind the cofactor, we aim to understand and explore redox behavior and mechanistic pathways of these systems. Using Rosetta, we designed well-packed protein scaffolds capable of binding the metallocorrole cofactor, optimizing both primary and secondary coordination sphere interactions. The designed protein, FEC-07, was spectroscopically characterized, confirming its ability to bind the cofactor (Fe(Cl)TPC, TPC = 5,10,15-triphenylcorrole) and enabling further exploration of its capacity to generate oxidative species. Due to the redox non-innocence of corroles the resting state of this metalloprotein is thought to be Fe(III)TPC•+. Initial results from UV-vis spectroscopy confirm binding of the metallocofactor to the protein, indicate formation of a new species after reaction with H2O2 which can be directed towards oxidation of guaiacol. As we move towards more complex substrates, we will interrogate the identity of this intermediate through electron paramagnetic resonance (EPR) and Mössbauer spectroscopy. There are no examples of Compound I-like species prepared in Fe-corroles therefore the ability to form Fe(IV)-oxo species within a designed protein would be a major advance in our understanding. Ultimately, the knowledge gained will support the designability of fully functional metalloproteins capable of accessing highly oxidizing species and pave the way for the development of functional metalloproteins designed entirely from scratch.