Oxidative stress is tightly regulated by cytochrome c phosphorylation and respirasome factors in mitochondria.

ABSTRACT: Respiratory cytochrome c has been found to be phosphorylated at tyrosine 97 in the postischemic brain upon neuroprotective insulin treatment, but how such posttranslational modification affects mitochondrial metabolism is unclear. Here, we report the structural features and functional behavior of a phosphomimetic cytochrome c mutant, which was generated by site-specific incorporation at position 97 of p-carboxymethyl-l-phenylalanine using the evolved tRNA synthetase method. We found that the point mutation does not alter the overall folding and heme environment of cytochrome c, but significantly affects the entire oxidative phosphorylation process. In fact, the electron donation rate of the mutant heme protein to cytochrome c oxidase, or complex IV, withi

SUBMITTER: Guerra-Castellano A 

PROVIDER: S-EPMC6077723 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature