Fig. 2: Acetylmimetic K39Q Cytc demonstrates altered rate of oxidation by H2O2, rate of reduction by superoxide, midpoint redox potential, and cardiolipin peroxidase activity. | Nature Communications

Fig. 2: Acetylmimetic K39Q Cytc demonstrates altered rate of oxidation by H2O2, rate of reduction by superoxide, midpoint redox potential, and cardiolipin peroxidase activity.

From: Cytochrome c lysine acetylation regulates cellular respiration and cell death in ischemic skeletal muscle

Fig. 2

A Initial rate of oxidation of reduced recombinant Cytc proteins by 100 μM H2O2 (n = 3). B Initial rate of reduction of oxidized recombinant Cytc proteins by superoxide generated with a hypoxanthine/xanthine oxidase system (n = 4). C Midpoint redox potentials of recombinant Cytc proteins were measured using the equilibration method with DCIP as the reference compound (n = 3). D Heme degradations of oxidized recombinant Cytc proteins after the addition of 3 mM H2O2 (n = 3). E Cardiolipin peroxidase activities of recombinant Cytc proteins with liposomes containing 0%, 20%, 30%, and 50% tetrazolyl-cardiolipin (TOCL) were measured using resorufin fluorescence after the addition of 5 μM H2O2 (n = 4). Data are represented as means ± standard deviation. A one-way ANOVA comparing the mean of each mutant with the mean of the control mutant (WT) with the Dunnett post-hoc test was used. For D, the 800 s condition specifically was compared.

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