title: Why does mitochondrial complex I have so many subunits?
abstract: The prokaryotic and eukaryotic homologues of complex I (proton-pumping NADH:quinone oxidoreductase) perform the same function in energy transduction, but the eukaryotic enzymes are twice as big as their prokaryotic cousins, and comprise three times as many subunits. Fourteen core subunits are conserved in all complexes I, and are sufficient for catalysis - so why are the eukaryotic enzymes embellished by so many supernumerary or accessory subunits? In this issue of the Biochemical Journal, Angerer et al. have provided new evidence to suggest that the supernumerary subunits are important for enzyme stability. This commentary aims to put this suggestion into context.
authors.affiliation: Medical Research Council Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Cambridge, UK. jh@mrc-mbu.cam.ac.uk
authors.forename: Judy
authors.initials: J
authors.lastname: Hirst
mesh_terms: D000818:Animals; D002417:Cattle; D042967:Electron Transport Complex I / Q000737:chemistry*; D004795:Enzyme Stability; D005057:Eukaryotic Cells / Q000201:enzymology; D008929:Mitochondria, Heart / Q000201:enzymology*; D011387:Prokaryotic Cells / Q000201:enzymology; D021122:Protein Subunits / Q000737:chemistry*
chemical_list: D021122:Protein Subunits; D042967:Electron Transport Complex I