Coordination compounds that mimic Purple Acid Phosphatases (PAPs) have drawn attention in the bioinorganic field due to their capacity to cleave phosphodiester bonds. However, their catalytic activity upon phosphate triesters is still unexplored. Thus, we report the synthesis and characterization of two binuclear complexes, MnIIMnIII(L1)(OAc)2BF4 (1) and MnIIFeIII(L1)(OAc)2BF4 (2) (H2L1 = 2-N,N-bis-(2- pyridilmethyl)aminomethyl-4-methyl-6-N-(2-hydroxy-3-formyl-5-methylbenzyl)-N-(2-pyridylmethyl)aminomethylphenol), their hydrolytic activity and antioxidant potential. The complexes were fully characterized, including the X-Ray diffraction (XRD) of 1. Density functional theory (DFT) calculations were performed to better understand their electronic and structural properties and phosphate conjugates. The catalytic activity was analyzed for two model substrates, a diester (BDNPP) and a triester phosphate (DEDNPP). The results suggest enhancement of the hydrolysis reaction by 170 to 1500 times, depending on the substrate and complex. It was possible to accompany the catalytic reaction of DEDNPP hydrolysis by phosphorus nuclear magnetic resonance (31P NMR), showing that both 1 and 2 are efficient catalysts. Moreover, we also addressed that 1 and 2 present a relevant antioxidant potential, protecting the yeast Saccharomyces cerevisiae, used as eukaryotic model of study, against the exposure of cells to acute oxidative stress. MnIIMnIII and FeIIIMnII complexes, their characterization, DFT studies and kinetics assays using a phosphate esters as substrates are reported. The results suggest enhancement of the hydrolysis reaction by 170 to 1500 times, depending on the system. We also addressed the relevant antioxidant potential, protecting cells against oxidative stress. Display omitted •Dinuclear complexes showed activity in the degradation of phosphate triester and diester.•The degradation reaction of phosphate esters were followed by 31P NMR.•FeIIIMnII and MnIIIMnII complexes protected cells against oxidative stress.