Abstract

This dataset contains data from the evaluation of the effect of S-allyl cysteine (SAC), Benzyl isothiocyanate (BITC), and Epicatechin (EPC) on mitochondria isolated from porcine hearts. The aim of the research was to verify the modulatory effect of the various molecules on mitochondrial bioenergetics through structure/activity correlation studies of the mitochondrial enzyme F1FO-ATPase, understand the involvement of the redox state on the induced effects, verify the kinetic parameters, and evaluate the effect on the phenomenon of the opening of the mitochondrial permeability transition pore (mPTP), involved in regulated cell death processes. The results, reported in “SAC_BITC_EPC_mitochondria_Dataset.xlsx”, show that it was possible to calculate Hill coefficients (nHi) for the hydrolytic activity of the Mg2+-activated enzyme in the absence and presence of BITC (“nHi_BITC” sheet) and SAC (“nHi_SAC” sheet), and for the Ca2+-activated enzyme in the absence and presence of BITC+ dithiothreitol (DTT) (“nHi_BITC_DTT_Ca_sub; “nHi_BITC_DTT_Ca_cof “ sheets). SAC showed an activating effect on Mg2+-activated F1FO-ATPase (“SAC_MgATPase” sheet) but not when activated by Ca2+ (“SAC_CaATPase” sheet) and its activating effect was lost in the presence of DTT (“SAC_MgATPaseDTT” sheet). BITC showed an inhibit effect on Mg2+-activated F1FO-ATPase (“BITC_MgATPase” sheet) but not when activated by Ca2+ (“BITC_CaATPase” sheet). In presence of DTT, the effect of BITC on Mg2+-activated enzyme was not modulated (“BITC_MgATPaseDTT” sheet) while it was enhanced on Ca2+-activated enzyme (“BITC_CaATPaseDTT” sheet). EPC did not alter Mg2+- (“EPC_MgATPase” sheet) or Ca2+-activated F1FO-ATPase (“EPC_CaATPase” sheet) in any way. SAC showed competitive activation for the cofactor Mg2+ (“Kinetics SAC_cofactorMg” sheet) and uncompetitive activation for the substrate ATP (“Kinetics SAC_substrateATP” sheet). BITC inhibited with a mixed-type mechanism towards the substrate (“Kinetics BITC_substrateATP” sheet) and the cofactor Mg2+ (“Kinetics BITC_cofactorMg” sheet). The inhibition of BITC on Ca2+-activated F1FO-ATPase exerted in the presence of DTT was found to be of mixed type towards the substrate ATP (“Kinetics BITC_substrate_Ca” sheet) and cofactor Ca2+ (“Kinetics BITC_cofactorCa” sheet). SAC and EPC did not alter mitochondrial respiration as assessed by Complex I of the electron transport chain (NADH-O2 oxidoreductase activity) and Complex II (SUCC-O2 oxidoreductase activity) (“SAC NADH-SUCC_O2”; “EPC NADH-SUCC_O2” sheets). BITC also inhibited respiration at high concentrations (“BITC NADH-SUCC_O2” sheet). The modulatory effect of SAC, BITC and EPC was also evaluated on CRC (“CRC” sheet), an index of mPTP opening.