Related Experiment Video
Updated: Aug 17, 2026

Synthesis and Evaluation of a Ruthenium-based Mitochondrial Calcium Uptake Inhibitor
Published on: October 26, 2017
Mitochondrial glycosidic residues contribute to the interaction between ruthenium amine complexes and the calcium
Francisco Correa1, Cecilia Zazueta
1Departamento de Bioquímica, Instituto Nacional de Cardiología Ignacio Chávez, México.
Abstract:
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.
Related Concept Videos
The Supercomplexes in the Crista Membrane
The Inner Mitochondrial Membrane
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
The Electron Transport Chain
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q in...
Mitochondrial Membranes

