Asymmetric organotellurides were chosen as potent antioxidants to construct a catalyst-protein conjugate called human serum albumin (HSA). Amino and methoxy group were known to increase catalytic activity, and compounds were found to be highly active and readily attachable to transport proteins. The activity of the agents in both assays were comparable, with second order rate constants for H2O2 reduction and zinc release. A reasonable correlation between electron-rich substituents, on the aromatic ring, the first oxidation potential, and catalytic activity of chalcogen compounds were shown using cyclic voltammetry. The results confirm that it is possible to load chemically simple, yet catalytically highly active enzyme mimics onto HSA.