Abstract

This dataset contains data from the evaluation of the inhibitory effect of dextromethorphan (DXM) on the hydrolytic and synthesis activity of mitochondrial F1FO-ATPase, isolated from porcine heart. The aim of the research was to investigate how DXM influences the catalysis of the enzyme, investigating the kinetic mechanisms by which it is expressed in order to understand how its toxicity can impact cellular mitochondrial activity. The file "DXM_F_ATPase_Dataset.zip" contains data relating to the effect of increasing concentrations of DXM on the hydrolytic activity of F1FO-ATPase ("Titration_curve.csv"). The inhibitory mechanism was investigated through enzyme kinetic studies ("Kinetic.csv"), further exploring the dynamics by which DXM interacts with the enzyme ("Time_course.csv"). The modulation of the enzymatic redox state was considered in relation to the inhibitory effect of DXM ("Reducing_agents.csv"). The hypothesis of a possible interaction of DXM on the hydrophobic portion of the FO enzyme was confirmed by mutual exclusion studies between DXM and a known inhibitor of the enzymatic activity that binds the ideophobic portion of FO, Dicyclohexylcarbodiimide DCCD ("Mutual_exclusion.csv"). Finally, the inhibitory effect of DXM on the synthesis activity of F1FO-ATPase, specifically on the oxidative phosphorylation (OXPHOS) process was confirmed ("OXPHOS.csv").