Reversible inactivation of dihydrolipoamide dehydrogenase by mitochondrial hydrogen peroxide.

ABSTRACT: Under oxidative stress conditions, mitochondria are the major site for cellular production of reactive oxygen species (ROS) such as superoxide anion and H2O2 that can attack numerous mitochondrial proteins including dihydrolipoamide dehydrogenase (DLDH). While DLDH is known to be vulnerable to oxidative inactivation, the mechanisms have not been clearly elucidated. The present study was therefore designed to investigate the mechanisms of DLDH oxidative inactivation by mitochondrial reactive oxygen species (ROS). Mitochondria, isolated from rat brain, were incubated with mitochondrial respiratory substrates such as pyruvate/malate or succinate in the presence of electron transport chain inhibitors such as rotenone or antimycin A. This is followed by enzyme activity assay and gel-based prote

SUBMITTER: Yan LJ 

PROVIDER: S-EPMC3690130 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature