Cardiolipin binding in bacterial respiratory complexes: Structural and functional implications

• Published in: Biochimica et biophysica acta 2012-10, Vol.1817 (10), p.1937-1949
• Main Authors: Arias-Cartin, Rodrigo, Grimaldi, Stéphane, Arnoux, Pascal, Guigliarelli, Bruno, Magalon, Axel
• Format: Article
• Language: English
• Subjects: Aerobic and anaerobic respiration; Bacteria; Bacteria - enzymology; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Biochemistry; Biochemistry, Molecular Biology; Cardiolipin; Cardiolipins - chemistry; Cardiolipins - metabolism; Crystallography, X-Ray; Electron-Transferring Flavoproteins; Formate dehydrogenase; Life Sciences; membrane proteins; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Nitrate reductase; phospholipids; photosynthesis; prokaryotic cells; Respiratory complex; signal transduction; solutes; X-radiation
• ISSN: 0005-2728; 0006-3002; 1879-2650
• DOI: 10.1016/j.bbabio.2012.04.005

The structural and functional integrity of biological membranes is vital to life. The interplay of lipids and membrane proteins is crucial for numerous fundamental processes ranging from respiration, photosynthesis, signal transduction, solute transport to motility. Evidence is accumulating that specific lipids play important roles in membrane proteins, but how specific lipids interact with and enable membrane proteins to achieve their full functionality remains unclear. X-ray structures of membrane proteins have revealed tight and specific binding of lipids. For instance, cardiolipin, an anionic phospholipid, has been found to be associated to a number of eukaryotic and prokaryotic respiratory complexes. Moreover, polar and septal accumulation of cardiolipin in a number of prokaryotes may ensure proper spatial segregation and/or activity of proteins. In this review, we describe current knowledge of the functions associated with cardiolipin binding to respiratory complexes in prokaryotes as a frame to discuss how specific lipid binding may tune their reactivity towards quinone and participate to supercomplex formation of both aerobic and anaerobic respiratory chains. This article is part of a Special Issue entitled: 17th European Bioenergetics Conference (EBEC 2012). ► Cardiolipin is a key component of energy-transducing membranes. ► Cardiolipin tunes the reactivity of the nitrate reductase complex towards quinone. ► Cardiolipin may influence quinone reactivity of the formate dehydrogenase complex. ► Polar and septal accumulation of cardiolipin is observed in bacteria. ► Cardiolipin binding may be at the origin of supercomplex formation in bacteria.