Abstract
Substantial evidence exists that the mitochondrial respiratory chain is organized in supramolecular units called supercomplexes or respirasomes. While the structural evidence of the supercomplexes is overwhelming, fewer studies have focused on their functional relevance. Although the presence of coenzyme Q channeling between complexes I and III has been ascertained, no such clear demonstration has been carried out for cytochrome c between complexes III and IV, at least in mammalian mitochondria. This review also discusses the implications concerning the number of respiratory complexes organized in supercomplexes and the possibility that they represent associations in dynamic equilibrium with the individual complexes.
©2013 by Walter de Gruyter Berlin Boston
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: European BioEnergetics Conference 2012 in Freiburg
- Highlight: European Bioenergetics Conference 2012 in Freiburg
- Structure of caa3 cytochrome c oxidase – a nature-made enzyme-substrate complex
- Recent advances in the electrochemistry and spectroelectrochemistry of membrane proteins
- pKa values and redox potentials of proteins. What do they mean?
- Cyclophilin D as a potential target for antioxidants in neurodegeneration: the X-ALD case
- A critical appraisal of the role of respiratory supercomplexes in mitochondria
- Mechanistic aspects of sodium-binding sites in LeuT-like fold symporters
- Hydroxynonenal-stimulated activity of the uncoupling protein in Acanthamoeba castellanii mitochondria under phosphorylating conditions
- The antiporter-like subunit constituent of the universal adaptor of complex I, group 4 membrane-bound [NiFe]-hydrogenases and related complexes
- Alternate pathways for NADH oxidation in Thermus thermophilus using type 2 NADH dehydrogenases
- A new trend in the complex I research field
- Research Articles/Short Communications
- Protein Structure and Function
- Expression in non-melanogenic systems and purification of soluble variants of human tyrosinase
- Chemical and enzymatic characterization of recombinant rabbit muscle pyruvate kinase
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: European BioEnergetics Conference 2012 in Freiburg
- Highlight: European Bioenergetics Conference 2012 in Freiburg
- Structure of caa3 cytochrome c oxidase – a nature-made enzyme-substrate complex
- Recent advances in the electrochemistry and spectroelectrochemistry of membrane proteins
- pKa values and redox potentials of proteins. What do they mean?
- Cyclophilin D as a potential target for antioxidants in neurodegeneration: the X-ALD case
- A critical appraisal of the role of respiratory supercomplexes in mitochondria
- Mechanistic aspects of sodium-binding sites in LeuT-like fold symporters
- Hydroxynonenal-stimulated activity of the uncoupling protein in Acanthamoeba castellanii mitochondria under phosphorylating conditions
- The antiporter-like subunit constituent of the universal adaptor of complex I, group 4 membrane-bound [NiFe]-hydrogenases and related complexes
- Alternate pathways for NADH oxidation in Thermus thermophilus using type 2 NADH dehydrogenases
- A new trend in the complex I research field
- Research Articles/Short Communications
- Protein Structure and Function
- Expression in non-melanogenic systems and purification of soluble variants of human tyrosinase
- Chemical and enzymatic characterization of recombinant rabbit muscle pyruvate kinase