New Evidence for the Multiplicity of Ubiquinone- and Inhibitor-Binding Sites in the Mitochondrial Complex I

2000 ◽  
Vol 381 (2) ◽  
pp. 241-246 ◽  
Author(s):  
José R. Tormo ◽  
Ernesto Estornell
Keyword(s):  
Binding Sites ◽  
Complex I ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Inhibitor Binding ◽  
New Evidence

Why does mitochondrial complex I have so many subunits?

2011 ◽  
Vol 437 (2) ◽  
pp. e1-e3 ◽  
Author(s):  
Judy Hirst
Keyword(s):  
Complex I ◽  
Enzyme Stability ◽  
Energy Transduction ◽  
Proton Pumping ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Nadh:Quinone Oxidoreductase ◽  
Biochemical Journal ◽  
Accessory Subunits ◽  
New Evidence

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.

The ND1 Subunit Constructs the Inhibitor Binding Domain in Bovine Heart Mitochondrial Complex I†

Biochemistry ◽  
2007 ◽  
Vol 46 (21) ◽  
pp. 6409-6416 ◽  
Author(s):  
Masatoshi Murai ◽  
Atsushi Ishihara ◽  
Takaaki Nishioka ◽  
Takao Yagi ◽  
Hideto Miyoshi
Keyword(s):  
Complex I ◽  
Binding Domain ◽  
Mitochondrial Complex I ◽  
Mitochondrial Complex ◽  
Inhibitor Binding ◽  
Bovine Heart
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