The apicomplexan parasite Toxoplasma gondii has a divergent mitochondrial electron transport chain (mETC). Complex III and IV associate together to form supercomplexes. We identified and deleted a Complex IV subunit (ApiCox10) which mediates this interaction. We perfomred immunoprecipitation of complex IV, via an HA epitope tagged Cox2a subunit in a parental and ApiCox10 knockout lines extracted in the mild detergent digitonin and analysed the elution via LFQ mass spectrometry. In the parental line, by immunoprecipitating Complex IV, complex III is also recovered, whereas in the ApiCox10 mutant only Complex IV is recovered due to impaired supercomplex formation.