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Cardiolipin is associated with the terminal oxidase of an extremely halophilic archaeon

Angela Corcelli1, Simona Lobasso, Luigi L Palese

  • 1Department of Medical Biochemistry, Medical Biology and Medical Physics, University of Bari, Bari, Italy. a.corcelli@biologia.uniba.it

Biochemical and Biophysical Research Communications
|February 3, 2007
PubMed

Membranes having an a high content of cardiolipin were isolated from an extremely halophilic archaeon Halorubrum sp. Absorbance difference spectra of detergent-solubilized plasma membranes reduced by dithionite suggested the presence of b-type cytochromes. Non-denaturing gel electrophoresis revealed only one fraction having TMPD-oxidase activity in which cardiolipin was the major lipid component. The electroeluted fraction showed a cytochrome c oxidase activity characterized by the reduced minus oxidized difference spectra as a terminal heme-copper oxidase. The cytochrome c oxidase activity of the archaeal cardiolipin-rich membranes was inhibited by the cardiolipin-specific fluorescent marker 10-N-nonyl acridine orange (NAO) in a dose-dependent manner. The results indicate that an archaeal analogue of cardiolipin is tightly associated to archaeal terminal oxidases and is required for its optimal functioning.

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