Artificial metalloenzymes are engineered proteins that contain a metal molecule that helps them carry out chemical reactions. The enzyme is considered artificial because it can perform a reaction outside of a living organism. These systems have gained interest due to their potential applications in green chemistry. Many current industrial methods rely on harsh conditions and toxic reagents. For example, making indigo can involve cyanide and high temperatures, which require a lot of energy and produce harmful byproducts such as isatin and anthranilic acid. Phenylethanol is often produced using aluminum chloride, a corrosive chemical that creates halogenated waste. Benzaldehyde is commonly synthesized using heavy metal oxidizing agents, which can generate oxidizing byproducts. In contrast, using enzymes allow reactions to be performed at a neutral pH, generate water as a byproduct, and avoid the use of toxic reagents common in current methods. Previous studies have shown that the artificial metalloenzyme LmrR containing an iron porphyrin cofactor can perform oxidation reactions by removing an electron and leaving behind a radical cation. In addition, mutations were introduced into LmrR to improve catalytic efficiency. In this study, we tested whether LmrR with a metal cofactor could perform additional reactions. The reaction mixtures contained a pH 7.5 buffer, an oxidant, a metal porphyrin, the LmrR protein, and a substrate. Indole, benzyl alcohol, and ethylbenzene were used in attempts to produce indigo, benzaldehyde, and phenylethanol. The reactions were analyzed using UV-Vis spectroscopy, GC-MS, and LC-MS. No detectable formation of the products was observed under the conditions tested, indicating further investigation under optimized reaction conditions is necessary to fully evaluate the potential of LmrR.