Mitochondrial glycosidic residues contribute to the interaction between ruthenium amine complexes and the calcium uniporter.

The role of glycosidic residues in the inhibitory properties of ruthenium complexes on mitochondrial calcium uptake was determined in mitoplasts. Our results showed that the binding and inhibitory properties of ruthenium amine complexes were modified when mitoplasts were exposed to N-glycosidase F action, but calcium uptake was not altered. N-linked proteins of the mitochondrial inner membrane were identified. We detected an 18-kDa protein that binds labeled Ru360 under control conditions, but failed to bind the inhibitor after deglycosilation. A relationship between this protein and the action of ruthenium amine inhibitors of the mitochondrial uniporter is proposed.