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Cardiolipin (CL) is a lipid that is found in the membranes of bacteria and the inner membranes of mitochondria. CL can increase the activity of integral membrane proteins, in particular components of respiratory pathways. We here report that CL activated detergent-solubilized cytochrome  bd,  a terminal oxidase from  Escherichia coli.  CL enhanced the oxygen consumption activity ~ twofold and decreased the apparent  K  M  value for ubiquinol-1 as substrate from 95 µM to 35 µM. Activation by CL was also observed for cytochrome  bd  from two Gram-positive species,  Geobacillus thermodenitrificans  and  Corynebacterium glutamicum,  and for cytochrome  bo  3  from  E. coli . Taken together, CL can enhance the activity of detergent-solubilized cytochrome  bd  and cytochrome  bo  3 .

Cardiolipin enhances the enzymatic activity of cytochrome bd and cytochrome bo3 solubilized in dodecyl-maltoside