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- Barbeau 2018 Biochem J + (The mechanisms regulating oxidative phosph … The mechanisms regulating oxidative phosphorylation during exercise remain poorly defined, however key mitochondrial proteins, including carnitine-palmitoyl transferase-I (CPT-I) and adenine-nucleotide translocase have redox sensitive sites. Interestingly muscle contraction has recently been shown to increase mitochondrial membrane potential and reactive oxygen species (ROS) production, therefore we aimed to determine if mitochondrial derived ROS influences bioenergetic responses to exercise. Specifically, we examined the influence of acute exercise on mitochondrial bioenergetics in WT and transgenic mice (MCAT) possessing attenuated mitochondrial ROS. We found that ablating mitochondrial ROS did not alter palmitoyl-CoA (P-CoA) respiratory kinetics or influence the exercise-mediated reductions in malonyl-CoA sensitivity, suggesting mitochondrial ROS does not regulate CPT-I. In contrast, while mitochondrial protein content, maximal coupled respiration, and ADP sensitivity in resting muscle were unchanged in the absence of mitochondrial ROS, exercise increased the apparent ADP Km (decreased ADP sensitivity) ~30% only in WT mice. Moreover, while the presence of P-CoA decreased ADP sensitivity, it did not influence the basic response to exercise, as the apparent ADP Km was increased only in the presence of mitochondrial ROS. This basic pattern was also mirrored in the ability of ADP to supress mitochondrial H<sub>2</sub>O<sub>2</sub> emission rates, as exercise decreased the suppression of H<sub>2</sub>O<sub>2</sub> only in WT mice. Altogether, these data demonstrate that while exercise-induced mitochondrial derived ROS does not influence CPT-I substrate sensitivity, it inhibits ADP sensitivity independent of P-CoA. These data implicate mitochondrial redox signalling as a regulator of oxidative phosphorylation.data implicate mitochondrial redox signalling as a regulator of oxidative phosphorylation.)
