Mitochondrial respiratory chain super-complex I-III in physiology and pathology. 2010

Giorgio Lenaz, and Alessandra Baracca, and Giovanna Barbero, and Christian Bergamini, and Maria Elena Dalmonte, and Marianna Del Sole, and Marco Faccioli, and Anna Falasca, and Romana Fato, and Maria Luisa Genova, and Gianluca Sgarbi, and Giancarlo Solaini
Dipartimento di Biochimica, Università di Bologna, Via Irnerio 48, 40126 Bologna, Italy.

Recent investigations by native gel electrophoresis showed the existence of supramolecular associations of the respiratory complexes, confirmed by electron microscopy analysis and single particle image processing. Flux control analysis demonstrated that Complex I and Complex III in mammalian mitochondria kinetically behave as a single unit with control coefficients approaching unity for each component, suggesting the existence of substrate channeling within the super-complex. The formation of this supramolecular unit largely depends on the lipid content and composition of the inner mitochondrial membrane. The function of the super-complexes appears not to be restricted to kinetic advantages in electron transfer: we discuss evidence on their role in the stability and assembly of the individual complexes, particularly Complex I, and in preventing excess oxygen radical formation. There is increasing evidence that disruption of the super-complex organization leads to functional derangements responsible for pathological changes, as we have found in K-ras-transformed fibroblasts.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008928 Mitochondria Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed) Mitochondrial Contraction,Mitochondrion,Contraction, Mitochondrial,Contractions, Mitochondrial,Mitochondrial Contractions
D008954 Models, Biological Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment. Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic
D004579 Electron Transport The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270) Respiratory Chain,Chain, Respiratory,Chains, Respiratory,Respiratory Chains,Transport, Electron
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000375 Aging The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time. Senescence,Aging, Biological,Biological Aging
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D014450 Electron Transport Complex III A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to UBIQUINONE, and transfers the electrons to CYTOCHROME C. In MITOCHONDRIA the redox reaction is coupled to the transport of PROTONS across the inner mitochondrial membrane. Complex III,Cytochrome bc1 Complex,Ubiquinol-Cytochrome-c Reductase,Coenzyme Q-Cytochrome-c Reductase,Coenzyme QH2-Cytochrome-c Reductase,Core I Protein, UCCreductase,Core I Protein, Ubiquinol-Cytochrome c Reductase,Core II Protein, UCCreductase,Core II Protein, Ubiquinol-Cytochrome c Reductase,Cytochrome b-c2 Oxidoreductase,Cytochrome bc1,Dihydroubiquinone-Cytochrome-c Reductase,QH(2)-Cytochrome-c Reductase,QH(2)-Ferricytochrome-c Oxidoreductase,Ubihydroquinone-Cytochrome-c Reductase,Ubiquinol-Cytochrome c Reductase,Ubiquinone-Cytochrome b-c2 Oxidoreductase,Coenzyme Q Cytochrome c Reductase,Coenzyme QH2 Cytochrome c Reductase,Core I Protein, Ubiquinol Cytochrome c Reductase,Core II Protein, Ubiquinol Cytochrome c Reductase,Cytochrome b c2 Oxidoreductase,Dihydroubiquinone Cytochrome c Reductase,Reductase, Ubiquinol-Cytochrome c,Ubihydroquinone Cytochrome c Reductase,Ubiquinol Cytochrome c Reductase,Ubiquinone Cytochrome b c2 Oxidoreductase
D017382 Reactive Oxygen Species Molecules or ions formed by the incomplete one-electron reduction of oxygen. These reactive oxygen intermediates include SINGLET OXYGEN; SUPEROXIDES; PEROXIDES; HYDROXYL RADICAL; and HYPOCHLOROUS ACID. They contribute to the microbicidal activity of PHAGOCYTES, regulation of SIGNAL TRANSDUCTION and GENE EXPRESSION, and the oxidative damage to NUCLEIC ACIDS; PROTEINS; and LIPIDS. Active Oxygen Species,Oxygen Radical,Oxygen Radicals,Pro-Oxidant,Reactive Oxygen Intermediates,Active Oxygen,Oxygen Species, Reactive,Pro-Oxidants,Oxygen, Active,Pro Oxidant,Pro Oxidants,Radical, Oxygen
D042963 Electron Transport Complex II A flavoprotein oxidase complex that contains iron-sulfur centers. It catalyzes the oxidation of SUCCINATE to fumarate and couples the reaction to the reduction of UBIQUINONE to ubiquinol. Succinate Dehydrogenase (Ubiquinone),Succinate Dehydrogenase-CoQ Reductase,Succinate Dehydrogenase-Coenzyme Q Reductase,Succinate-Coenzyme Q Reductase,Succinate-Q Oxidoreductase,Succinate-Quinone Oxidoreductase,Succinate-Ubiquinone Oxidoreductase,Succinate-Ubiquinone Reductase,Dehydrogenase-CoQ Reductase, Succinate,Oxidoreductase, Succinate-Q,Oxidoreductase, Succinate-Quinone,Oxidoreductase, Succinate-Ubiquinone,Reductase, Succinate Dehydrogenase-CoQ,Succinate Coenzyme Q Reductase,Succinate Dehydrogenase CoQ Reductase,Succinate Dehydrogenase Coenzyme Q Reductase,Succinate Q Oxidoreductase,Succinate Quinone Oxidoreductase,Succinate Ubiquinone Oxidoreductase,Succinate Ubiquinone Reductase

Related Publications

Giorgio Lenaz, and Alessandra Baracca, and Giovanna Barbero, and Christian Bergamini, and Maria Elena Dalmonte, and Marianna Del Sole, and Marco Faccioli, and Anna Falasca, and Romana Fato, and Maria Luisa Genova, and Gianluca Sgarbi, and Giancarlo Solaini
August 1985, Biochemical Society transactions,
Giorgio Lenaz, and Alessandra Baracca, and Giovanna Barbero, and Christian Bergamini, and Maria Elena Dalmonte, and Marianna Del Sole, and Marco Faccioli, and Anna Falasca, and Romana Fato, and Maria Luisa Genova, and Gianluca Sgarbi, and Giancarlo Solaini
November 2010, Zhonghua er ke za zhi = Chinese journal of pediatrics,
Giorgio Lenaz, and Alessandra Baracca, and Giovanna Barbero, and Christian Bergamini, and Maria Elena Dalmonte, and Marianna Del Sole, and Marco Faccioli, and Anna Falasca, and Romana Fato, and Maria Luisa Genova, and Gianluca Sgarbi, and Giancarlo Solaini
February 1981, The Journal of biological chemistry,
Giorgio Lenaz, and Alessandra Baracca, and Giovanna Barbero, and Christian Bergamini, and Maria Elena Dalmonte, and Marianna Del Sole, and Marco Faccioli, and Anna Falasca, and Romana Fato, and Maria Luisa Genova, and Gianluca Sgarbi, and Giancarlo Solaini
July 2008, Molecular and cellular biochemistry,
Giorgio Lenaz, and Alessandra Baracca, and Giovanna Barbero, and Christian Bergamini, and Maria Elena Dalmonte, and Marianna Del Sole, and Marco Faccioli, and Anna Falasca, and Romana Fato, and Maria Luisa Genova, and Gianluca Sgarbi, and Giancarlo Solaini
April 2018, Seminars in cell & developmental biology,
Giorgio Lenaz, and Alessandra Baracca, and Giovanna Barbero, and Christian Bergamini, and Maria Elena Dalmonte, and Marianna Del Sole, and Marco Faccioli, and Anna Falasca, and Romana Fato, and Maria Luisa Genova, and Gianluca Sgarbi, and Giancarlo Solaini
November 2011, Zhonghua er ke za zhi = Chinese journal of pediatrics,
Giorgio Lenaz, and Alessandra Baracca, and Giovanna Barbero, and Christian Bergamini, and Maria Elena Dalmonte, and Marianna Del Sole, and Marco Faccioli, and Anna Falasca, and Romana Fato, and Maria Luisa Genova, and Gianluca Sgarbi, and Giancarlo Solaini
April 2002, Nihon rinsho. Japanese journal of clinical medicine,
Giorgio Lenaz, and Alessandra Baracca, and Giovanna Barbero, and Christian Bergamini, and Maria Elena Dalmonte, and Marianna Del Sole, and Marco Faccioli, and Anna Falasca, and Romana Fato, and Maria Luisa Genova, and Gianluca Sgarbi, and Giancarlo Solaini
January 2017, Cell metabolism,
Giorgio Lenaz, and Alessandra Baracca, and Giovanna Barbero, and Christian Bergamini, and Maria Elena Dalmonte, and Marianna Del Sole, and Marco Faccioli, and Anna Falasca, and Romana Fato, and Maria Luisa Genova, and Gianluca Sgarbi, and Giancarlo Solaini
June 2017, Fetal and pediatric pathology,
Giorgio Lenaz, and Alessandra Baracca, and Giovanna Barbero, and Christian Bergamini, and Maria Elena Dalmonte, and Marianna Del Sole, and Marco Faccioli, and Anna Falasca, and Romana Fato, and Maria Luisa Genova, and Gianluca Sgarbi, and Giancarlo Solaini
November 2006, Revista espanola de anestesiologia y reanimacion,
Copied contents to your clipboard!