Succinate and phenylsuccinate as modifiers of sulfhydryl groups of inner mitochondrial membrane protein. Study by EPR.
Paramagnetic labels specific for sulfhydryl (SH) groups have been used to study the conformational changes of the inner mitochondrial membrane. The EPR spectra of the SH-groups spin-labeled with maleimide or iodoacetamide show the existence of two populations of sulfhydryl groups, differing in their mobility (one weakly, the other strongly immobilized). The incubation with succinate or phenylsuccinate decreased the binding of these labels of the weakly immobilized sites while the number of total SH groups was the same before and after the incubation. These results suggest that succinate or phenylsuccinate induce a reversible change in protein conformation or in protein arrangement within the inner mitochondrial membrane. This change is concomitant to the protein movement between inner membrane and perimembranal space induced by either of these two molecules.
D000818:Animals; D004578:Electron Spin Resonance Spectroscopy; D007425:Intracellular Membranes / Q000032:analysis*; D008565:Membrane Proteins / Q000032:analysis*; D008930:Mitochondria, Liver / Q000032:analysis*; D011487:Protein Conformation; D051381:Rats; D013386:Succinates; D019802:Succinic Acid; D013438:Sulfhydryl Compounds / Q000032:analysis
D008565:Membrane Proteins; D013386:Succinates; D013438:Sulfhydryl Compounds; C017625:2-phenylsuccinate; D019802:Succinic Acid