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MitoNEET is a mitochondrial iron-sulfur protein with poorly-understood functions. Proposed functions of mitoNEET include regulating of oxidative capacity, reactive oxygen homeostasis, and other possible roles. Investigating the interactions of mitoNEET with other proteins might help identify functional roles of this protein. MitoNEET was discovered in 2004 to identify physiological targets of pioglitazone hydrochloride, a drug that is commonly used to treat type-2 diabetes. Type-2 diabetes is a metabolic disease and, although the exact pathology is complex, the role of the mitochondrion in cellular energy production and glucose oxidation indicates that this organelle has a role in type-2 diabetes. Because of the specific location of mitoNEET and its interaction with pioglitazone, there is the potential for this protein to have a role in diabetes treatment and/or prevention. My protein pull-down experiments indicated a direct interaction between mitoNEET and the enzyme catalase, which decomposes hydrogen peroxide (H2O2). Ultraviolet-visible spectroscopy of catalase, before and after the addition of mitoNEET, showed changes in absorbance at λ = 270, 320 and 400 nm, indicating an interaction between the proteins. The rate of catalase activity was measured by following the breakdown of H2O2 over time. The average rate of catalase activity in absence of mitoNEET was 0.0899 ± 0.0195 nM H2O2 min-1 μg protein-1 and this rate increased after addition of mitoNEET to 0.0126 ± 0.0253 nM H2O2 min-1 μg protein-1. My findings may indicate that mitoNEET decreases cellular H2O2 levels through activation of catalase, and thereby reduces the probability to develop oxidative stress induced insulin resistance.