Skip to main content
    • Aa
    • Aa

The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains

  • John E. Walker (a1)

The inner membranes of mitochondria contain three multi-subunit enzyme complexes that act successively to transfer electrons from NADH to oxygen, which is reduced to water (Fig. I). The first enzyme in the electron transfer chain, NADH:ubiquinone oxidoreductase (or complex I), is the subject of this review. It removes electrons from NADH and passes them via a series of enzyme-bound redox centres (FMN and Fe-S clusters) to the electron acceptor ubiquinone. For each pair of electrons transferred from NADH to ubiquinone it is usually considered that four protons are removed from the matrix (see section 4.1 for further discussion of this point).

Hide All
Albracht S. P. J., Dooijewaard G., Leeuwerik F. J. & Van Swol B. (1977). EPR signals of NADH: Q oxidoreductase shape and intensity. Biochim. biophys. Acta 459, 300317.
Albracht S. P. J., Leeuwerik F. J. & Van Swol B. (1979). The stoichiometry of the iron-sulphur clusters ia, ib and 2 of NADH:Q oxidoreductase as present in beef heart submitochondrial particles. FEBS Lett. 104, 197200.
Albracht S. P. J. & Barker P. T. A. (1986). Evidence for two independent pathways of electron transfer in mitochondrial NADH:Q oxidoreductase. II. Kinetics of reoxidation of the reduced enzyme. Biochim. biophys. Acta 850, 423428.
Alex L. I., Reeve J. N., Orme-Johnson W. H. & Walsh C. T. (1990). Cloning, sequence determination and expression of the genes encoding the subunits of the nickel containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautrophicum ΔH. Biochemistry 29, 72377244.
Anderson S., Bankier A. T., Barrell B. G., De Bruijn M. H. L., Coulson A. R., Drouin J., Eperon I. C., Nierlich D. D., Roe B. A., Sanger F., Schreier P. H., Smith A. J. H., Staden R. & Young I. G. (1981). Sequence and organization of the human mitochondrial genome. Nature 290, 457465.
Anderson S., De Bruijn M. H. L., Coulson A. R., Eperon I. C., Sanger F. & Young I. G. (1982). Complete sequence of bovine mitochondrial DNA. J. molec. Biol. 156, 683717.
Andrews K. M., Crofts A. R. & Gennis R. B. (1990). Large-Scale Purification and characterisation of a highly active four-subunit cytochrome bc 1 complex from Rhodobacter sphaeroides. Biochemistry 29, 26452651.
Arizmendi J. M., Runswick M. J., Skehel J. M. & Walker J. E. (1992). NADH: ubiquinone oxidoreductase from bovine heart mitochondria: a fourth nuclear coded subunit with a homologue encoded in chloroplast genomes. FEBS Lett. 301, 237242.
Arnason U., Gullberg A. & Widegren B. (1991). The complete nucleotide sequence of the mitochondrial DNA of the fin whale, Balaenoptera physalus. J. molec. Evol. 33, 556568.
Babcock G. T. & Wikström M. (1992). Oxygen activation and the conservation of energy in cell respiration. Nature 356, 301308.
Baccarini-Melandri A., Zannoni D. & Melandri B. A. (1973). Energy transduction in photosynthetic bacteria. VI. Respiratory sites of energy conservation in membranes from dark grown cells of Rhodopseudomonas capsulata. Biochim. biophys. Acta 314, 298311.
Bakker P. T. A. & Albracht S. P. J. (1986). Evidence for two independent pathways of electron transfer in mitochondrial NADH:Q oxidoreductase. I. Pre-steady state kinetics with NADPH. Biochim. biophys. Acta 850, 413422.
Ballinger S. W., Shoffner J. M., Hedaya E. V., Trounce I., Polak M. A., Koontz D. A. & Wallace D. C. (1992). Maternally transmitted diabetes and deafness associated with a 10–4 kb mitochondrial DNA deletion. Nature Genetics 1, 1115.
Batuecas B., Garesse R., Calleja M., Valverde J. R. & Marco R. (1988). Genome organization of Artemia mitochondrial DNA. Nucl. Acids Res. 16, 65156529.
Beavis A. D. (1987). Upper and lower limits of the charge translocation stoichiometry of mitochondrial electron transport, j. biol. Chem. 262, 61656173.
Beinert H. & Albracht S. P. J. (1982). New insights, ideas and unanswered questions concerning iron–sulphur clusters in mitochondria. Biochim. biophys. Ada 683, 245277.
Benecke R., Strümper P. & Weiss H. (1992). Electron transfer complex I defect in idiopathic dystonia. Ann. Neurol. (in the press).
Bennoun P. (1982). Evidence for a respiratory chain in the chloroplast. Proc. natn. Acad. Sci. USA 79, 43524356.
Berger S., Ellersiek U. & Steinmüller K. (1991). Cyanobacteria contain a mitochondrial complex I – homologous NADH dehydrogenase. FEBS Lett. 286, 129132.
Berks B. B. & Ferguson S. J. (1991). Simplicity and complexity of electron transfer between NADH and c-type cytochromes in bacteria. Biochem. Soc. Trans. 19, 581588.
Bibb M. J., Van Etten R. A., Wright C. T., Walberg M. W. & Clayton D. A. (1981). Sequence and organization of mouse mitochondrial DNA. Cell 26, 167180.
Bindoff L. A., Birch-Machin M., Cartlidge N. E. F., Parker W. D. & Turnbull D. M. (1989). Mitochondrial function in Parkinson's disease. Lancet ii, 49.
Boehnke M., Conneally P. M. & Lange K. (1983). Two models for a maternal factor in the inheritance of Huntington's disease. Am. J. Hum. Genet. 35, 845860.
Boekema E. J., Van Breemen J. F. L., Keegstra W., Van Bruggen E. J. E. & Albracht S P. J. (1982). Structure of NADH:Q oxidoreductase from bovine heart mitochondria studies by electron microscopy. Biochim. biophys. Ada 679, 711.
Böhm R., Sauter M. & Böck (1990). Nucleotide sequence and expression of an operon in Escherichia colt coding for formate hydrogenylase components. Mol. Microbiol. 4, 231243.
Botstein D. (1980). A theory for molecular evolution of bacteriophages. Ann. N.Y. Acad. Sci. 354, 484491.
Breakefield X. O. (1992). Molecular approaches to diseases of the nervous system. In An Introduction to Molecular Neurobiology (ed. Hall Z. W.), pp. 517. Sunderland, Mass., U.S.A.: Sinauer Associates, Inc.
Brink J., Hovmöller S., Ragan C. I., Cleeter M. W. J., Boekema E. J. & Van Bruggen E. F. J. (1987). The structure of NADH:ubiquinone oxidoreductase from beef-heart mitochondria. Crystals containing an octameric arrangement of ironsulphur protein fragments. Eur. J. Biochem. 166, 287294.
Brody S. & Mikolajczyk S. (1988). Neurospora mitochondria contain an acyl-carrier protein. Eur. J. Biochem. 173, 353359.
Brody S., Mikolajczyk S. & Chuman L. (1990). Studies on de novo fatty acid synthesis in mitochondria. In Plant Lipid Biochemistry, Structure and Utilization (ed. Quinn P. J. et al. ), pp. 117119. London: Harwood, Portland Press Limited.
Brown G. C. & Brand M. D. (1988). Proton/electron stoichiometry of mitochondrial complex I estimated from the equilibrium thermodynamic force ratio. Biochem. J. 252, 473479.
Brown M. D., Voljavec A. S., Lott M. T., Torroni A., Yang C. C. & Wallace D. C. (1992). Mitochondrial DNA complex I and II mutations associated with Leber's hereditary optic neuropathy. Genetics 130, 163173.
Brusilow W. S. A., Scarpetta M. A., Hawthorne C. A. & Clark W. P. (1989). Organization and sequence of the genes encoding the proton-translocating ATPase of Bacillus megaterium. J. biol. Chem. 264, 15281533.
Burbaev D. Sh, Moroz I. A., Kotlyar A. B., Sled V. D. & Vinogradov A. D. (1989). Ubisemiquinone in the NADH-ubiquinone reductase region of the mitochondrial respiratory chain. FEBS Lett. 254, 4751.
Burger G. & Werner S. (1986). The mitochondrial URFi gene in Neurospora crassa has an intron that contains a novel kind of URF. J. molec. Biol. 186, 231242.
Cammack R. (1992). Iron-sulphur clusters in enzymes – themes and variations. Adv. Inorg. Chem. 38, 281322.
Cantatore P., Roberti M., Rainaldi G., Gadaleta M. N. & Saccone C. (1989). The complete nucleotide sequence, gene organization and genetic code of the mitochondrial genome of Paracentrotus lividus. J. biol. Chem. 264, 1096510975.
Carducci C. Leuzzi V., Scuderi M., De Negri A. M., Gabrieli C. B., Antonozzi I. & Pontecorvi A. (1991). Mitochondrial DNA mutation in an Italian family with Leber hereditary optic neuropathy. Hum. Genet. 87, 725727.
Casjens S. & Hendrix R. (1974). Comments on the arrangement of the morphogenetic genes of bacteriophage lambda. J. molec. Biol. 90, 2023.
Chen S. & Guillory R. J. (1981). Studies on the interaction of arylazido-β alanyl NAD+ with the mitochondrial NADH dehydrogenase. J. biol. Chem. 256, 83188323.
Chen S. & Guillory R. J. (1984). Identification of the NADH-NAD+ transhydrogenase peptide of the mitochondrial NADH-CoQ reductase (complex I). A photodependent labeling study utilizing arylazido-β-alanyl NAD+. J. biol. Chem. 259, 51245131.
Chomyn A., Mariottini P., Gonzalez-Cadavid N., Attardi G., Strong D. D., Trovato D., Riley M. & Doolittle R. F. (1983). Identification of the polypeptides encoded in the ATPase 6 gene and in the unassigned reading frames 1 and 3 of human mt DNA. Proc. natn. Acad. Sci. USA 80, 55355539.
Chomyn A., Mariottini P., Cleeter M. W. J., Ragan C. I., Matsuno-Yagi A., Hatefi Y., Doolittle R. F. & Attardi G. (1985). Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature 314, 592597.
Chomyn A., Cleeter M. W. J., Ragan C. I., Riley M., Doolittle R. F. & Attardi G. (1986). URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit. Science 234, 614618.
Chomyn A., Meola G., Bresolin N., Lai S. T., Scarlato G. & Attardi G. (1991). In vitro genetic transfer of protein synthesis and respiration defects to mitochondrial DNA-less cells with myopathy patient mitochondria. Molec. Cell Biol. II, 22362244.
Chow W., Ragan C. I. & Robinson B. H. (1991). Determination of the cDNA sequence for the human mitochondrial 75 kDa Fe-S protein of NADH coenzyme Q reductase. Eur.J. Biochem. 201, 547550.
Ciafaloni E., Ricci E., Shanske S., Moraes C. T., Sivestri G., Hirano M., Simonetti S., Angelini C., Donati M. A., Garcia C., Martinuzzi A., Mosewich R., Servidei S., Zammarchi E., Bonilla E., De Vivo D. C., Rowland L. P., Schon E. A. & Dimauro S. (1992). MELAS: clinical features, biochemistry, and molecular genetics. Ann. Neurol. 31, 391398.
Clary D. O. & Wolstenholme D. R. (1985). The mitochondrial DNA molecule of Drosophila yakuba: nucleotide sequence, gene organization and genetic code. J. molec. Evol. 22, 252271.
Cooper J. M., Schapira A. H. V., Holt I. J., Toscano A., Harding A. E., Morgan-Hughes J. A. & Clark J. B. (1990). Biochemical and molecular aspects of human mitochondrial respiratory chain disorders. Biochem. Soc. Trans. 18, 517519.
Coppel R. L., McNeilage L. J., Surh C. D., Van De Water J., Spithill T. W., Whittingham S. & Gershwin M. E. (1988). Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis: dihydrolipoamide acetyltransferase. Proc. natn. Acad. Sci. USA 85, 73177321.
Correll C. C. & Ludwig M. L. (1991). Structure determination of an iron-sulfur flavoprotein. In Flavins and Flavoproteins (ed. Curti B. et al. ), pp. 743747. Berlin: Walter de Gruyter.
Cozens A. L. & Walker J. E. (1987). The organization and sequence of the genes for ATP synthase subunits in the cyanobacterium Synechococcus 6301: support for an endosymbiotic origin of chloroplasts. j. molec. Biol. 194, 359383.
Cozens A. L., Walker J. E., Phillips A. L., Huttly A. K. & Gray J. C. (1986). A sixth subunit of ATP synthase, an F0 component, is encoded in the pea chloroplast genome. EMBO J. 5, 217222.
Cremona T. & Kearney E. B. (1964). Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. J. biol. Chem. 239, 23282334.
Cummings D. J., McNally K. L., Domenico J. M. & Matsuura E. T. (1990). The complete DNA sequence of the mitochondrial genome of Podospora anserina. Curr. Genet. 17, 375402.
De Jonge P. C. & Westerhoff H. V. (1982). The proton-per-electron stoichiometry of ‘site I’ of oxidative phosphorylation at high protonmotive force is close to 1·5. Biochem. J. 204, 515523.
De Pamphilis C. W. & Palmer J. D. (1990). Loss of photosynthetic and chlororespiratory genes from the plastid genome of a parasitic flowering plant. Nature 348, 337339.
De Vries S. & Marres C. A. M. (1987). The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism. Biochim. biophys. Acta 895, 205239.
De Vries S. & Grivell L. A. (1988). Purification and characterisation of a rotenoneinsensitive NADH: Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae. Eur. J. Biochem. 176, 377384.
Deng P. S. K., Hatefi Y. & Chen S. (1990). N-Arylazido-β-alanyl-NAD+, a new NAD+ photoaffinity analogue. Synthesis and labeling of mitochondrial NADH dehydrogenase. Biochemistry 29, 10941098.
Denovan-Wright E. M. & Lee R. W. (1992). Comparative analysis of the mitochondrial genomes of Chlamydomonas eugametos and Chlamydomonas moewusii. Curr. Genet. 21, 197202.
Desjardins P. & Morais R. (1990). Sequence and gene organization of the chicken mitochondrial genome: a novel gene order in higher vertebrates. J. molec. Biol. 212, 599634.
Di Virgilio F. & Azzone G. F. (1982). Activation of site I redox driven H+ pump by exogenous quinones in intact mitochondria. J. biol. Chem. 257, 41064113.
Dimroth P. & Thomer A. (1989). A primary respiratory Na+ pump of an anaerobic bacterium: the Na+-dependent NADH:quinone oxidoreductase of Klebsiella pneumoniae. Arch. Microbiol. 151, 439444.
Dooijewaard G. & Slater E. C. (1976a). Steady state kinetics of high molecular weight (type I) NADH dehydrogenase. Biochim. Biophys. Acta 440, 115.
Dooijewaard G. & Slater E. C. (1976 b). Steady state kinetics of low molecular weight (type-II) NADH dehydrogenase. Biochim. biophys. Acta 440, 1635.
Dupuis A. (1992). Identification of two genes of Rhodobacter capsulatus coding for proteins homologous to the NDi and 23 kDa subunits of the mitochondrial complex. FEBS Lett. 301, 215218.
Dupuis A., Skehel J. M. & Walker J. E. (1991 a). Plant chloroplast genomes encode a homologue of a nuclear coded iron–sulfur protein subunit of bovine mitochondrial complex I. Biochemistry 30, 29542960.
Dupuis A., Skehel J. M. & Walker J. E. (1991 b). NADH:ubiquinone reductase from bovine mitochondria: complementary DNA sequence of a 19 kDa cysteine rich subunit. Biochem. J. 277, 1115.
Earley F. G. P. & Ragan C. I. (1984). Photoaffinity labelling of mitochondrial NADH dehydrogenase with arylazidomorphigenin, an analogue of rotenone. Biochem. j. 224, 525534.
Earley F. G. P., Patel S. D., Ragan C. I. & Attardi G. (1987). Photolabelling of a mitochondrially encoded subunit of NADH dehydrogenase with [3H]dihydrorotenone. FEBS Lett. 219, 108113.
Eklund H., Samana J. P., Wallén L., Brändén C. I., Åkeson Å. & Jones T. A. (1981). Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 29 Å resolution. J. molec. Biol. 146, 561587.
Engel W. D., Schägger H. & Von Jagow G. (1983). Isolation of complex III from various mitochondria. Comparison of the structural and functional properties of the preparations from beef heart, calf liver and Neurospora crassa. Hoppe Seyler's Z. Physiol. Chem. 364, 17531763.
Esser U., Krumholz L. R. & Simoni R. D. (1990). Nucleotide sequence of the F0 subunits of the sodium dependent F1F0, ATPase of Propionigenium modestum. Nucl. Acids Res. 18, 5887.
Falk G. & Walker J. E. (1988). DNA sequence of a gene cluster coding for subunits of the Fo membrane sector of ATP synthase in Rhodospirillum rubrum. Biochem. j. 254, 109122.
Fearnley I. M. & Walker J. E. (1987). Initiation codons in mammalian mitochondria: differences in the genetic code of the organelle. Biochemistry 26, 82478251.
Fearnley I. M., Runswick M. J. & Walker J. E. (1989). A homologue of the nuclear encoded 49 kD subunit of bovine mitochondrial NADH-unbiquinone reductase is coded in chloroplast DNA. EMBO J. 8, 665672.
Fearnley I. M., Finel M., Skehel J. M. & Walker J. E. (1991). NADH: ubiquinone oxidoreductase from bovine heart mitochondria; cDNA sequences of the import precursors of the nuclear coded 39-kDa and 42-kDa subunits. Biochem. J. 278, 821829.
Fearnley I. M. & Walker J. E. (1992). Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins. Biochim. Biophys. Acta Bioenerget. Revs (in the press).
Fenn J. B., Mann M., Meng C. K., Wong S. F. & Whitehouse C. M. (1989). Electrospray ionization for mass spectrometry of large biomolecules. Science 246, 6171.
Filser M. & Werner S. (1988). Pethidine analogues, a novel class of potent inhibitors of mitochondrial NADH: ubiquinone reductase. Biochem. Pharmacol. 37, 25512558.
Finel M., Skehel J. M., Albracht S. P. J., Fearnley I. M. & Walker J. E. (1992). Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes one of which contains the redox centres of the enzyme. Biochemistry (in the press).
Friedrich T., Hofhaus G., Ise W., Nehls U., Schmitz B. & Weiss H. (1989). A small isoform of NADH:ubiquinone oxidoreductase (complex I) without mitochondrially synthesized subunits is made in chloramphenicol treated Neurospora crassa. Eur.J. Biochem. 180, 173180.
Friedrich T., Strohdeicher M., Hofhaus G., Preis D., Sahm H. & Weiss H. (1990). The same domain motif for ubiquinone reduction in mitochondrial or chloroplast NADH dehydrogenase and bacterial glucose dehydrogenase. FEBS Lett. 265, 374O.
Frostell Å, Mendel-Hartvig I., Nelson B. D., Tötterman T. H., Björkland A. & Ragan C. I. (1988). Evidence that the major primary biliary cirrhosis-specific mitochondrial autoantigen is a subunit of complex I of the respiratory chain. Scandjf. Immunol. 28, 157165.
Fukushima T., Decker R. V., Anderson W. M. & Spivey H. O. (1989). Substrate channeling of NADH and binding of dehydrogenases to complex I. J. biol. Chem. 264, 1648316488.
Fussey S. P. M., Guest J. R., James O. F. W., Bassendine M. F. & Yeaman S. J. (1988). Identification and analysis of the major M2 autoantigens in primary biliary cirrhosis. Proc. natn. Acad. Sci. USA 85, 86548658.
Gadaleta G., Pepe G., De Candida G., Quagliariello E., Sbisa E. & Saccone V. (1989). The complete nucleotide sequence of the Rattus norvegius mitochondrial genome: cryptic signals revealed by comparative analysis between vertebrates. J. molec. Evol. 28, 497516.
Galante Y. M. & Hatefi Y. (1979). Purification and molecular properties of mitochondrial NADH dehydrogenase. Arch. Biochem. Biophys. 192, 559568.
Garab G., Lajkó F., Mustárdy L. & Márton L. (1989). Respiratory control over photosynthetic electron transport in chloroplasts of higher plant cells: evidence for chlororespiration. Planta 179, 349358.
Garesse R. (1988). Drosophila melanogaster mitochondrial DNA: gene organization and evolutionary considerations. Genetics 118, 649663.
Gerth K., Jansen R., Reifenstahl G., Höfle G., Irschik H., Kunze B., Reichenbach H. & Thierbach G. (1983). The myxalamids, new antibiotics from Myxococcus xanthus (myxobacterales). I. Production, physico-chemical and biological properties, and mechanism of action. J. Antibiotics 36, 11501156.
Gibb G. M. & Ragan C. I. (1990). Identification of the subunits of bovine NADH dehydrogenase which are encoded in the mitochondrial genome. Biochem. J. 265, 903906.
Godde D. (1982). Evidence for a membrane bound NADH-plastoquinone-oxidoreductase in Chlamydomonas reinhardii CW-15. Arch. Microbiol. 131, 197202.
Godde D. & Trebst A. (1980). NADH as electron donor for the photosynthetic membrane of Chlamydomonas reinhardii. Arch. Microbiol. 127, 245252.
Gordon J. I., Duronio R. J., Rudnick D. A., Adams S. P. & Gokel G. W. (1991). Protein N-myristoylation. j. biol. Chem. 266, 86478650.
Goto Y., Nonaka I. & Horai S. (1991). A new mtDNA mutation associated with mitochondrial myopathy, encephalopathy, lactic acidosis and stroke-like episodes (MELAS). Biochim. biophys. Acta 1097, 238240.
Graham L. A. & Trumpower B. L. (1991). Mutational analysis of the mitochondrial Rieske iron–sulfur protein of Saccharomyces cerevisiae. III Import, protease processing, and assembly into the cytochrome bci complex of iron–sulfur protein lacking the iron–sulfur cluster. J. biol. Chem. 266, 2248522492.
Gusella J. F., Wexler N. S., Coneally P. M., Naylor S. L., Anderson M. A., Tanzi R. E., Watkins P. C., Ottina K., Wallace M. R., Sakaguchi A. Y., Young A. B., Shoulsen I., Bonilla E. & Martin J. B. (1983). A polymorphic DNA marker genetically linked to Huntington's Disease. Nature 306, 234238.
Harding A. E., Holt I. J., Cooper J. M., Schapira A. H. V., Sweeney M., Clark J. B. & Morgan-Hughes J. A. (1990). Mitochondrial myopathies: genetic defects. Biochem. Soc. Trans. 18, 519523.
Harnisch U., Weiss H. & Sebald W. (1985). The primary structure of the iron–sulfur subunit of ubiquinol-cytochorme c reductase from Neurospora, determined by cDNA and gene sequencing. Eur. J. Biochem. 149, 9599.
Hase T., Wakabayashi S., Matsubara H., Imai T., Matsumoto T. & Tobari J. (1979). Mycobacterium smegmatis ferredoxin: a unique distribution of cysteine residues constructing iron–sulfur clusters. FEBS Lett. 103, 224228.
Hatefi Y. (1985). The mitochondrial electron transport and oxidative phosphorylation system. Ann. Rev. Biochem. 54, 10151069.
Hatefi Y., Haavik A. G. & Griffiths D. E. (1962). Studies on the electron transfer system. XL. Preparation and properties of mitochondrial DPNH-coenzyme Q reductase. J. biol. Chem. 237, 16761680.
Hawlitschek G., Schneider H., Schmidt B., Tropschug M., Hartl F. U. & Neupert W. (1988). Mitochondrial protein import. Identification of the processing peptidase and of PEP, a processing enhancing protein. Cell 53, 795806.
Hayashi M. & Unemoto T. (1986). FAD and FMN flavoproteins participate in the sodium transport respiratory chain NADH: quinone reductase of a marine bacterium, Vibrio alginolyticus. FEBS Lett. 202, 327330.
Hayashi M. & Unemoto T. (1987). Subunit composition and their roles in the sodium transport NADH:quinone reductase of a marine bacterium, Vibrio alginolyticus. Biochim. biophys. Ada 890, 4754.
Hayashi M., Miyoshi T., Takashina S. & Unemoto T. (1989). Purification of NADH-ferricyanide dehydrogenase and NADH-quinone reductase from Escherichia coli membranes and their roles in the respiratory chain. Biochim. biophys. Acta 977, 6269.
Hiratsuka J., Shimada H., Whittier R., Ishibashi T., Sakamoto M., Mori M., Kondo C., Honji Y., Sun C. R., Meng B. Y., Li Y. Q., Kanno A., Nishizawa Y., Hirai A., Shinozaki K. & Sugiura M. (1989). The complete sequence of the rice (Oryza sativa) chloroplast genome: intermolecular recombination between distinct tRNA genes accounts for a major plastic DNA inversion during the evolution of the cereals. Mol. Gen. Genet. 217, 185194.
Hockenbery D., Nuñez G., Mllliman C., Schreiber R. D. & Korsmeyer S. (1990). Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 348, 334336.
Hockenbery D. M., Zutter M., Hlckey W., Nahm M. & Korsmeyer S. J. (1991). BCL2 protein is topographically restricted in tissues characterized by apoptotic cell death. Proc. natn. Acad. Sci. USA 88, 69616965.
Hofhaus G., Weis H. & Leonard K. (1991). Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I). J. molec. Biol. 221, 10271043.
Høj P. B., Svendsen I., Scheller H. V. & Møler B. L. (1987). Identification of a chloroplast encoded 9 kDa polypeptide as a 2[4Fe-4S] protein carrying centers A and B of photosystem I. j. biol. Chem. 262, 1267612684.
Holt I. J., Harding A. E. & Morgan-Hughes J. A. (1988). Deletions of muscle mitochondrial DNA in patients with mitochondrial myopathies. Nature 331, 717719.
Howell N., Kubacka I., Xu M. & McCullough D. A. (1991). Leber hereditary optic neuropathy: involvement of the mitochondrial NDi gene and evidence for an intragenic suppressor mutation. Am. J. Hum. Genet. 48, 935942.
Howell N., McCullough D. & Bodis-Wollner I. (1992). Molecular genetic analysis of a sporadic case of Leber hereditary optic neuropathy. Am. J. Hum. Genet. 50, 443446.
Huoponen K., Vilkki J., Aula P., Nikoskelainen E. K. & Savontaus M. L. (1991). A new mt DNA mutation associated with Leber hereditary optic neuropathy. Am.J. Hum. Genet. 48, 11471153.
Hwang S-R & Tabita F. R. (1991). Acyl carrier protein derived sequence encoded by the chloroplast genome in the marine diatom Cylindrotheca sp. strain Ni. J. biol. Chem. 266, 1349213494.
Ingledew W. J. & Ohnishi T. (1980). An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria. Biochem. J. 186, 111117.
Ise W., Haiker H. & Weiss H. (1985). Mitochondrial translation of subunits of the rotenone-sensitive NADH:ubiquinone reductase in Neurospora crassa. EMBO J. 4, 20752080.
Ivey D. M. & Krulwich T. A. (1991). Organization and nucleotide sequence of the atp genes encoding the ATP synthase from alkaliphilic Bacillus firmus OF4. Mol. Gen. Genet. 229, 292300.
Hacobs H. T., Elliott D. J., Math V. B. & Farquharson A. (1988). Nucleotide sequence and gene organization of sea urchin mitochondrial DNA. J. molec. Biol. 202, 185217.
Jaiswal A. K., Burnett P., Adesnik M. & McBride O. W. (1990). Nucleotide and deduced amino acid sequence of a human cDNA (NQO2) corresponding to a second member of the NAD(P)H:quinone oxidoreductase gene family. Extensive polymorphism at the NQO2 gene locus on chromosome 6. Biochemistry 29, 18991906.
Johansen S., Guddal P. H. & Johansen T. (1990). Organization of the mitochondrial genome of Atlantic cod, Gadus morhua. Nucleic Acids Res. 18, 411419.
Johns D. R. & Berman J. (1991). Alternative, simultaneous complex I mitochondrial DNA mutations in Leber's hereditary optic neuropathy. Biochem. Biophys. Res. Commun. 174, 13241330.
Jörnvall H. (1977). Differences between alcohol dehydrogenases: structural properties and evolutionary aspects. Eur. J. Biochem. 72, 443452.
Karplus P. A., Daniels M. J. & Herriott J. R. (1990). Ferredoxin NADP+ reductase: prototype for a structurally novel flavoprotein family. Science 251, 6066.
Katayama M., Tanaka M., Yamamoto H., Ohbayashi T., Nimura Y. & Ozawa T. (1991). Deleted mitochondrial DNA in the skeletal muscle of aged individuals. Biochem Inter. 25, 4756.
Kikuno R. & Miyata T. (1985). Sequence homologies among mitochondrial DNAcoded URF2, URF4 and URF5. FEBS Lett. 189, 8588.
Kormann B. A., Schuster H., Berninger T. A. & Leo-Kottler B. (1991). Detection of the G to A mitochondrial DNA mutation at position 11778 in German families with Leber's hereditary optic neuropathy. Hum. Genet. 88, 98100.
Kotlyar A. B. & Vinogradov A. D. (1990). Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase. Biochim. biophys. Ada 1019, 151158.
Kotlyar A. B., Sled V. D., Burbaev D. Sh, Moroz I. A. & Vinogradov A. D. (1990). Coupling site I and the rotenone-sensitive ubisemiquinone in tightly coupled submitochondrial particles. FEBS Lett. 264, 1720.
Kotlyar A. B., Sled V. D. & Vinogradov A. D. (1992). Effect of Ca2+ ions on the slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase. Biochim. biophys. Ada 1098, 144150.
Kriauciunas A., Yu L., Yu C. A., Wynn R. M. & Knaff D. B. (1989). The Rhodospirillwn rubrum cytochrome bc 1 complex: peptide composition, prosthetic group content and quinone binding. Biochim. biophys. Ada 976, 7076.
Krishnamoorthy G. & Hinkle P. C. (1988). Studies on the electron transfer pathway, topography of iron–sulphur centres, and site of coupling in NADH-Q oxidoreductase. J. biol. Chetn. 263, 1756617575.
Krumholz L. R., Esser U. & Simoni R. D. (1989). Nucleotide sequence of the unc operon of Vibrio alginolyticus. Nucl. Acids Res. 17, 7993.
Laemmli U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680685.
Lakin-Thomas P. L. & Brody S. (1985). A pantothenate derivative is covalently bound to mitochondrial proteins in Neurospora crassa. Eur.J. Biochem. 146, 141147.
Lemasters J. J. (1984). The ATP to oxygen stoichiometries of oxidative phosphorylation by rat liver mitochondria. An analysis of ADP-induced oxygen jumps by linear nonequilibrium thermodynamics. J. biol. Chetn. 259, 1312313130.
Lemasters J. J., Grunwald R. & Emaus R. K. (1984). Thermodynamic limits to the ATP/site stoichiometries of oxidative phosphorylation by rat liver mitochondria, j. biol. Client. 259, 30583063.
Leonard K., Haiker H. & Weiss H. (1987). Three dimensional structure of NADH: ubiquinone reductase (complex I) from Neurospora mitochondria determined by electron microscopy of membrane crystals. J. Molec. Biol. 194, 277286.
Lestienne P., Nelson J., Riederer P., Jellinger K. & Reichmann H. (1990). Normal mitochondrial genome in brain from patients with Parkinson's disease and complex I defect., J. Neurochem. 55, 18101812.
Lim L. W., Shamala N., Mathews F. S., Steenkamp D. J., Hamlin R. & Xuong N. H. (1986). Three-dimensional structure of the iron–sulfur flavoprotein trimethylamine dehydrogenase at 2.4 Å resolution. J. biol. Chem. 261, 1514015146.
Lin F.-H, Lin R., Wisniewski H. M., Hwang Y.-W, Grundke-Iqbal I., Healylouie G. & Iqbal K. (1992). Detection of point mutations in codon 331 of mitochondrial NADH dehydrogenase subunit 2 in Alzheimer's brains. Biochem. biophys. Res. Commun. 182, 238246.
Lindqvist Y. (1989). Refined structure of spinach glycolate oxidase at 2 Å resolution. J. molec. Biol. 209, 151166.
Linnane A. W., Marzuki S., Ozawa T. & Tanaka M. (1989). Mitochondrial DNA mutations as an important contributor to ageing and degenerative diseases. Lancet i, 642645.
Lott M. T., Voljavec A. S. & Wallace D. C. (1990). Variable genotype of Leber's hereditary optic neuropathy patients. Am. J. Ophthalmol. 109, 625631.
Lutz S., Jacobi A., Schlensog R., Böhm R., Sawers G. & Böck A. (1991). Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli. Molec. Microbiol. 5, 123135.
Luu-The V., Lachance Y., Labrie C., Leblanc G., Thomas J. L., Strickler R. C. & Labrie F. (1989). Full length cDNA structure and deduced amino acid sequence of human 3β-hydroxy-5-ene steroid dehydrogenase. Molec. Endocrinol. 3, 13101312.
Maione T. E. & Gibbs M. (1986). Association of the chloroplastic respiratory chains of Chlamydomonas reinhardtii with photoreduction and the oxyhydrogen reaction. Plant Physiol. 80, 364368.
Majander A., Huoponen K., Savontaus M. L., Nikoskelainen E. & Wikström M. (1991). Electron transfer properties of NADH:ubiquinone reductase in the ND1/3460 and the ND4/11778 mutations of the Leber hereditary optic neuroretinopathy (LHON). FEBS Lett. 292, 289292.
Mann V. M., Cooper J. M., Javoy-Agid F., Agid Y., Jenner P. & Schapira A. H. V. (1990). Mitochondrial function and parental sex effect in Huntington's disease. Lancet 336, 749.
Martin C. E. & Johnston A. M. (1983). Changes in fatty acid distribution and thermotropic properties of phospholipids following phosphatidylcholine depletion in a choline requiring mutant of Neurospora crassa. Biochim. biophys. Acta 730, 1016.
Masui R., Wakabayashi S., Matsubara H. & Hatefi Y. (1991a). The amino acid sequences of two 13 kDa polypeptides and partial amino acid sequence of 30 kDa polypeptide of complex I from bovine heart mitochondria: possible location of iron–sulfur clusters. J. Biochem. 109, 534543.
Masui R., Wakabayashi S., Matsubara H. & Hatefi Y. (1991 b). The amino acid sequence of the 9 kDa polypeptide and partial amino acid sequence of the 20 kDa polypeptide of the mitochondrial NADH:ubiquinone oxidoreductase. J. Biochem. 110, 575582.
Mathews F. S. (1991). New flavoproteins. Current Opinion in Struct. Biol. 1, 954967.
Matsubayashi T., Wakasugi T., Shinozaki K., Yamaguchi-Shinozaki K., Zaita N., Hidaka T., Meng B. Y., Ohto C., Tanaka A., Maruyama T. & Sugiura M. (1987). Six chloroplast genes (ndh A-F) homologous to human respiratory chain NADH dehydrogenase are actively expresed. Mol. Gen. Genet. 210, 385393.
Mayes S. R., Cook K. M. & Barber J. (1990). Nucleotide sequence of the second psbG gene in Synechocystis 6803: possible implications for psb G function as a NAD(P)H dehydrogenase subunit gene. FEBS Lett. 262, 4954.
Mayhew S. G. & Ludwig M. (1975). Flavodoxins and electron-transferring flavoproteins. In The Enzymes (ed. Boyer P. D.), pp. 57118. New York: Academic Press.
McCarn D. F., Whitaker R. A., Alam J., Vrba J. M. & Curtis S. E. (1988). Genes encoding the alpha, gamma, detla, and four F0 subunits of ATP synthase constitute an operon in the cyanobacterium Anabaena sp. strain PCC 7120. J. Bact. 170, 34483458.
Meinhardt S., Kula T., Yagi T., Lillich T. & Ohnishi T. (1987). EPR characterization of the iron–sulfur clusters in the NADH: ubiquinone oxidoreductase segment of the respiratory chain in Paracoccus denitrificans. J. biol. Chem. 262, 91479153.
Meinhardt S. W., Matsushita K., Kaback H. R. & Ohnishi T. (1989). EPR characterization of the iron–sulfur containing NADH-ubiquinone oxidoreductase of the Escherichia coli aerobic respiratory chain. Biochemistry 28, 21532160.
Meinhardt S. W., Wang D. C., Koyu H., Yagi T., Oshima T. & Ohnishi T. (1990). Studies of the NADH-menaquinone oxidoreductase segment of the respiratory chain in Thermus thermophilus HB-8. J. biol. Chem. 265, 13601368.
Meng B. Y., Matsubayashi T., Wakasugi T., Shinozaki K., Sugiura M., Hirai A., Mikami T., Kishima Y. & Kinoshita T. (1986). Ubiquity of the genes for components of a NADH dehydrogenase in higher plant chloroplast genomes. Plant Sci. 47, 181184.
Mikolajczyk S. & Brody S. (1990). De novo fatty acid synthesis mediated by acylcarrier protein in Neurospora crassa mitochondria. Eur.J. Biochem. 187, 431437.
Mitchell P. (1966). Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Biol. Reviews 41, 455502.
Mizuno Y., Ohta S., Tanaka M., Takamiya S., Suzuki K., Sato T., Oya H., Ozawa T. & Kagawa Y. (1989). Deficiencies in complex I subunits of the respiratory chain in Parkinson's disease. Biochem. biophys. Res. Commun. 163, 14501455.
Moraes C. T., Dimauro S., Zeviani M., Lombes A., Shanske S., Miranda A. F., Nakase H., Bonila E., Werneck L. C., Servidei S., Nonaka I., Koga Y., Spiro A. J., Brownell K. W., Schmidt B., Schotland D. L., Zupanc M., De Vivo D. C., Schon E. A. & Rowland L. P. (1989). Mitochondrial DNA deletions in progressive external ophthalmoplegia and Kearns-Sayre syndrome. New Engl. j. med. 320, 12931299.
Moras D., Olsen K. W., Sabesan M. N., Buehner M., Ford G. C. & Rossmann M. G. (1975). Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase. J. biol. Chem. 290, 91379162.
Müller-Hocker J. (1989). Cytochrome c oxidase deficient cardiomyocytes in the human heart – an age-related phenomenon. Am. J. Pathol. 134, 11671173.
Murphy M. P. & Brand M. D. (1987). Variable stoichiometry of proton pumping by the respiratory chain. Nature 329, 170172.
Nakagawa-Hattori Y., Yoshino H., Kondo T., Mizuno Y. & Horai S. (1992). Is Parkinson's disease a mitochondrial disorder? J. Neurol. Sci. 107, 2933.
Nakahashi Y., Taketani S., Okuda M., Inoue K. & Tokunaga R. (1990). Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase. Biochem. biophys. Res. Commun. 173, 748755.
Nehls U., Hemmer S., Rühlen D. A., Van Der Pas J. C., Preis D., Sackmann U. & Weiss H. (1991). cDNA and genomic DNA sequence of the 21.3 kDa subunit of NADH: ubiquinone reductase (complex I) from Neurospora crassa. Biochim. biophys. Acta 1088, 325326.
Nehls U., Friedrich T., Schmiede A., Ohnishi T. & Weiss H. (1992). Characterization of assembly intermediates of NADH:ubiquinone oxidoreductase (complex I) accumulated in Neurospora mitochondria by gene disruption. J. molec. Biol. (in the press).
Nelson M. A. & Macino G. (1987). Structure and expression of the overlapping ND4L and ND5 genes of Neurospora crassa mitochondria. Molec. Gen. Genet. 206, 307317.
Nicholls D. G. & Ferguson S. J. (1992). In Bioenergetics, vol. 2. London and San Diego: Academic Press.
Nixon P. J., Gounaris K., Coomber S. A., Hunter C. N., Dyer T. A. & Barber J. (1989). psbG is not a photosystem two gene but may be an ndh gene. J. biol. Chem. 264, 1412914135.
Nohl H. (1987). Demonstration of the existence of an organo-specific NADH dehydrogenase in heart mitochondria. Eur.J. Biochem. 169, 585591.
Oda K., Yamato K., Ohta E., Nakamura Y., Takemura M., Nozato N., Akashi K., Kanege T., Ogura Y., Kohchi T. & Ohyama K. (1992). Gene organisation deduced from the complete sequence of liverwort Marchantia polymorpha mitochondrial DNA. A primitive form of plant mitochondrial DNA. J. molec. Biol. 223, 17.
Ohnishi T. (1975). Thermodynamic and EPR characterisation of iron–sulphur centres in the NADH-ubiquinone segment of the mitochondrial respiratory chain in pigeon heart. Biochim. biophys. Acta 387, 475490.
Ohnishi T. (1979). Mitochondrial iron–sulphur flavodehydrogenases. In Membrane Proteins in Energy Transduction (Ed. Capaldi R. A.), pp. 187. New York: Dekker.
Ohnishi T., Blum H., Galante Y. M. & Hatefi Y. (1981). Iron–sulfur clusters studied in NADH-ubiquinone oxidoreductase and in soluble NADH dehydrogenase. J. biol. Chem. 256, 92169220.
Ohnishi T., Ragan C. I. & Hatefi Y. (1985). EPR studies of iron–sulfur clusters in isolated subunits and subfractions of NADH-ubiquinone oxidoreductase. J. biol. Chem. 260, 27822788.
Oh-Oka H., Takahashi Y., Wada K., Matsubara H., Ohyama K. & Ozeki H. (1987). The 8 kDa polypeptide in photosystem I is a probable candidate of an iron sulphur protein coded by the chloroplast gene frxA. FEBS Lett. 218, 5254.
Ohta S., Yohda M., Ishizuka M., Hirata H., Hamamoto T., Otawarahamamoto Y., Matsuda K. & Kagawa Y. (1988). Sequence and over-expression of subunits of adenosine triphosphate synthase in thermophilic bacteria. Biochim. biophys. Acta. 933, 141155.
Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K., Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H. & Ozeki H. (1986). Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA. Nature 322, 571574.
Okimoto R., Macfarlane J. L., Clary D. O. & Wolstenholme D. R. (1992). The mitochondrial genomes of two nematodes, Caenorhabditis elegans and Ascaris suum. Genetics 130, 471498.
Orme-Johnson N. R., Hansen R. & Beinert H. (1974). Electron paramagnetic resonance detectable electron acceptors in beef heart mitochondria. Reduced diphosphopyridine nucleotide ubiquinone reductase segment of the electron transfer system. J. biol. Chem. 249, 19221927.
Paech C., Friend A. & Singer T. P. (1982). Simplified isolation and molecular composition of NADH dehydrogenase of the respiratory chain. Biochem. J. 203, 477481.
Parker W. D., Boyson S. J. & Parks J. K. (1989a). Abnormalities of the electron transport chain in idiopathic Parkinson's disease. Ann. Neurol. 26, 719723.
Parker W. D., Oley C. A. & Parks J. K. (1989b). A defect in mitochondrial electrontransport activity (NADH-coenzyme Q oxidoreductase) in Leber's hereditary optic neuropathy. New Engl. J. Med. 320, 13311333.
Parker W. D., Filley C. M. & Parks J. K. (1990 a). Cytochrome oxidase deficiency in Alzheimer's disease. Neurology 40, 13021303.
Parker W. D., Boyson S. J., Luder A. S. & Parks J. K. (1990 b). Evidence for a defect in NADH:ubiquinone oxidoreductase (complex I) in Huntington's disease. Neurology 40, 12311234.
Patel S. D., Aebersold R. & Attardi G. (1991). cDNA-derived amino acid sequence of the NADH-binding 51 kDa subunit of the bovine respiratory NADH de hydrogenase reveals striking similarities to a bacterial NAD+-reducing hydrogenase. Proc. natn. Acad. Sci. USA 88, 42254229.
Peck H. D. & Gest H. (1957). Formic dehydrogenase and the hydrogenylase enzyme complex in coli-aerogenes bacteria. J. Bacteriol. 73, 706721.
Peltier G., Ravenel J. & Verméglio A. (1987). Inhibition of a respiratory activity by short saturating flashes in Chlamydomonas: evidence for a chlororespiration. Biochim. biophys. Acta 893, 8390.
Pilkington S. J. & Walker J. E. (1989). Mitochondrial NADH-ubiquinone reductase: complementary DNA sequences of import precursors of the bovine and human 24 kDa subunit. Biochemistry 28, 32573264.
Pilkington S. J., Skehel J. M., Gennis R. B. & Walker J. E. (1991 a). Relationship between mitochondrial NADH-ubiquinone reductase and a NAD,+ reducing dehydrogenase. Biochemistry 30, 21662175.
Pilkington S. J., Skehel J. M. & Walker J. E. (1991 b). Plant chloroplast genomes encode a homologue of the nuclear coded 30 kDa subunit of bovine mitochondrial complex I. Biochemistry 30, 19011908.
Pollock R. A., Hartl F. U., Cheng M. Y., Ostermann J., Horwich A. & Neupert W. (1988). The processing peptidase of yeast mitochondria: the two cooperating components MPP and PEP are structurally related. EMBO J. 7, 34933500.
Poulton J., Deadman M. E., Bronte-Stewart J., Foulds W. S. & Gardiner R. M. (1991). Analysis of mitochondrial DNA in Leber's hereditary optic neuropathy. J. Med. Genet. 28, 765770.
Pozzan T., Miconi V., Di Virgilio F. & Azzone G. F. (1979). H+/site, charge/site, and ATP/site ratios at coupling sites I and II in mitochondrial etransport. J. biol. Chem. 254, 1020010205.
Preis D., Van Des Pas J. C., Nehls U., Röhlen D., Sackmann U., Jahnke U. & Weiss H. (1990). The 49 kDa subunit of NADH:ubiquinone reductase (complex I) from Neurospora crassa mitochondria: primary structure of the gene and the protein. Curr. Genet. 18, 5964.
Preis D., Weidner U., Conzen C., Azevedo J. E., Nehls U., Röhlen D. A., Van Der Pas J., Sackmann U., Schneider R., Werner S. & Weiss H. (1991). Primary structure of two subunits of NADH: ubiquinone reductase (complex I) from Neurospora crassa mitochondria: relationship to a soluble NAD-reducing hydrogenase from Alcaligenes eutrophus. Biochim. biophys. Acta 1090, 133138.
Pritchard A. E., Venuti S. E., Ghlalmbor M. A., Sable C. L. & Cummings D. J. (1989). An unusual region of Paramecium mitochondrial DNA containing chloroplast-like genes. Gene 78, 121134.
Pritchard A. E., Seilhamer J. J., Mahalingam R., Sable C. L., Venuti S. E. & Cummings D. J. (1990). Nucleotide sequence of the mitochondrial genome of Paramecium. Nucl. Acids Res. 18, 173180.
Purvis D. J., Theiler R. & Niederman R. A. (1990). Chromatographic and protein chemical analysis of the ubiquinol-cytochrome c 2 oxidoreductase isolated from Rhodobader sphaeroides. J. biol. Chem. 265, 12081215.
Ragan C. I. (1976). NADH ubiquinone oxidoreductase. Biochim. biophys. Acta 456, 249290.
Ragan C. I. (1987). Structure of NADH-ubiquinone reductase (complex I). Curr. Topics Bioenerget. 15, 136.
Ragan C. I. (1990). Structure and function of an archetypal respiratory chain complex: NADH-ubiquinose reductase. Biochem. Soc. Trans. 18, 515516.
Ragan C. I., Galante Y. M., Hatefi Y. & Ohnishi T. (1982 a). Resolution of mitochondrial NADH dehydrogenase and the isolation of two iron–sulfur proteins. Biochemistry 21, 590594.
Ragan C. I., Galante Y. M. & Hatefi Y. (1982 b). Purification of three iron–sulfur proteins from the iron-protein fragment of mitochondrial NADH-ubiquinone oxidoreductase. Biochemistry 21, 25182524.
Rawlings N. D. & Barrett A. J. (1991). Homologues of insulinase, a new superfamily of metalloendopeptidases. Biochem. J. 275, 389391.
Reanney D. C. & Ackermann H. W. (1985). Comparative biology and evolution of bacteriophages. Adv. Virus Res. 27, 205280.
Roe B. A., MA D-P., Wilson R. K. & Wong J. F. H. (1985). The complete nucleotide sequence of the Xenopus laevis mitochondrial genome. J. biol. Chem. 260, 97599774.
Röhlen D. A., Hoffmann J., Van Der Pas J. C., Nehls U., Preis D., Sackman U. & Weiss H. (1991). Relationship between a subunit of NADH dehydrogenase (complex I) and a protein family including subunits of cytochrome reductase and processing protease from mitochondria. FEBS Lett. 278, 7578.
Rose R. E., Dejesus C. E., Moylan S. L., Ridge N. P., Scherer D. E. & Knauf V. C. (1987). The nucleotide sequence of a cDNA clone encoding acyl carrier protein (ACP) from Brassica campestris seeds. Nucl. Acids Res. 15, 7197.
Rossman M. G., Liljas A., Bränden C. I. & Banaszak L. J. (1975). Evolutionary and structural relationships among dehydrogenases. In The Enzymes (ed. Boyer P. D.), pp. 61102. New York: Academic Press.
Rottenberg H. & Gutman M. (1977). Control of the reverse electron transport in submitochondrial particles by the free energy. Biochemistry 16, 32203227.
Runswick M. J., Gennis R. B., Fearnley I. M. & Walker J. E. (1989). Mitochondrial NADH:ubiquinone reductase: complementary DNA sequence of the import precursor of the bovine 75 kDa subunit. Biochemistry 28, 94529459.
Runswick M. J., Fearnley I. M., Skehel J. M. & Walker J. E. (1991). Presence of an acyl carrier protein in NADH:ubiquinone oxidoreductase from bovine heart mitochondria. FEBS Lett. 286, 121124.
Rutherfurd K. J., Chen S. & Shively J. E. (1991). Isolation and amino acid sequence analysis of bovine adrenal 3β-hydroxysteroid dehydrogenase/steroid isomerase. Biochemistry 30, 81088116.
Rypniewski W. R., Bretter D. R., Benning M. M., Wesenberg G., Oh B. H., Marhley J. L., Rayment I. & Holden H. M. (1991). Crystallization and structure determination to 2.5 Å resolution of the oxidised [2Fe-2S] ferredoxin isolated from Anabaena 7120. Biochemistry 30, 41264131.
Sackmann U., Zensen R., Röhlen D., Jahnke U. & Weiss H. (1991). The acyl carrier protein in Neurospora crassa mitochondria is a subunit of NADH: ubiquinone reductase (complex I). Eur. J. Biochem. 200, 463469.
Salerno J. C., Ohnishi T., Lim J., Widger R. & King T. E. (1977). Spin coupling between electron carriers in the dehydrogenase segments of the respiratory chain. Biochem. biophys. Res. Commun. 75, 618624.
Saraste M. (1990). Structural features of cytochrome c oxidase. Q. Rev. Biophys. 23, 321366.
Sawers R. G., Ballantine S. P. & Boxer D. H. (1985). Differential expression of hydrogenase isoenzymes in Escherichi coli K12: evidence for a third isoenzyme. J. Bacteriol. 164, 13241331.
Sawers R. G., Jamieson D. J., Higgins C. F. & Boxer D. H. (1986). Characterisation and physiological roles of membrane-bound hydrogenase isoenzymes from Salmonella typhimurium. J. Bacteriol. 168, 398404.
Schagger H. & Von Jagow G. (1987). Tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1-look Da. Anal. Biochem. 166, 368379.
Schapira A. H. V., Cooper J. M., Dexter D., Jenner P., Clark J. B. & Marsden C. D. (1989). Mitochondrial complex I deficiency in Parkinson's disease. Lancet i, 1269.
Schapira A. H. V., Cooper J. M., Dexter D., Clark J. B., Jenner P. & Marsden C. D. (1990). Mitochondrial complex I deficiency in Parkinson's disease. J. Neurochem. 54, 823827.
Scherer S. (1990). Do photosynthetic and respiratory electron transport chains share redox proteins? Trends Biochem. Sci. 15, 458462.
Schlame M., Beyer K., Hayer-Hartl M. & Klingenberg M. (1991). Molecular species of cardiolipin in relation to other mitochondrial phospholipids. Is there an acyl specificity of the interaction between cardiolipin and the ADP/ATP carrier? Eur. J. Biochem. 199, 459466.
Schmitt M. E. & Trumpower B. L. (1991). The petite phenotype resulting from a truncated copy of subunit 6 results from loss of assembly of the cytochrome bc 1 complex and can be suppressed by overexpression of subunit 9. J. biol. Chem. 266, 1495814963.
Schneider K., Cammack R., Schlegel H. G. & Hall D. O. (1979). The iron-sulphur centres of soluble hydrogenase from Alcaligenes eutrophus. Biochim. biophys. Acta 578, 445461.
Schneider K., Cammack R. & Schlegel H. G. (1984). Content and localisation of FMN, Fe-S clusters and nickel in the NAD-linked hydrogenase of Nocardia opaca Ib. Eur. jf. Biochem. 142, 7584.
Scholes T. A. & Hinkle P. C. (1984). Energetics of ATP-driven reverse electron transfer from cytochrome c to fumarate and from succinate to NAD in submitochondrial particles. Biochemistry 23, 33413345.
Schulte U., Arretz M., Schneider H., Tropschug M., Wachter E., Neupert W. & Weiss H. (1989). A family of mitochondrial proteins involved in bioenergetics and biogenesis. Nature 147, 147149.
Scrutton N. S., Berry A. & Perham R. N. (1990). Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature 343, 3843.
Shimomura Y., Kawada T. & Suzuki M. (1989). Capsaicin and its analogs inhibit the activity of NADH-coenzyme Q oxidoreductase of the mitochondrial respiratory chain. Arch. Biochem. Biophys. 270, 573577.
Shinozaki K., Ohme M., Tanaka M., Wakasugi T., Hayashida N., Matsubayashi T., Zaita N., Chunwongse J., Obokata J., Yamaguchi-Shinozaki K., Ohto C., Torazawa K., Meng B. Y., Sugita M., Deno H., Kamogashira T., Yamada K., Kusuda J., Takaiwa F., Kato A., Tohdoh N., Shimada H. & Sugiura M. (1986). The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression. EMBO J. 5, 20432049.
Shoffner J. M., Lott M. T., Lezza A. M. S., Seibel P., Ballinger S. W. & Wallace D. C. (1990). Myoclonic epilepsy and ragged-red fiber disease (MERRF) is associated with a mitochondrial DNA tRNALys mutation. Cell 61, 931937.
Shoffner J. M., Watts R. L., Juncos J. L., Torroni A. & Wallace D. C. (1991). Mitochondrial oxidative phosphorylation defects in Parkinson's disease. Ann. Neurol. 30, 332339.
Shoubridge E. A., Karpati G. & Hastings E. M. (1990). Deletion mutants are functionally dominant over wild-type mitochondrial genomes in skeletal muscle fiber segments in mitochondrial disease. Cell 62, 4349.
Shuber A. P., Orr E. C., Reeney M. A., Schendel P. F., May H. D., Schauer N. L. & Ferry J. G. (1986). Cloning, expression, and nucleotide sequence of the formate dehydrogenase genes from Methanobacterium formicicum. J. biol. Chem. 261, 1294212947.
Simpson L., Neckelman N., De La Cruz V. F., Simpson A. M., Feagin J. E., Jasmer D. P. & Stuart K. (1987). Comparison of the maxicircle (mitochondrial) genomes of Leishmania tarentolae and Trypanosoma brucei at the level of nucleotide sequence. J. biol. Chem. 262, 61826196.
Singer T. P. & Ramsay R. R. (1990). Mechanism of the neurotoxicity of MPTP. FEBS Lett. 274, 18.
Singer T. P. & Ramsay R. R. (1992). NADH-ubiquinone oxidoreductase. In Molecular Mechanisms in Bioenergetics (ed. Ernster L.). Amsterdam: Elsevier. (in the press).
Singer T. P., Trevor A. J. & Castagnoli N. (1987). Biochemistry of the neurotoxic action of MPTP: or how a faulty batch of ‘designer drug’ led to parkinsonism in drug abusers. TIBS 12, 266270.
Skehel J. M., Pilkington S. J., Runswick M. J., Fearnley I. M. & Walker J. E. (1991). NADH: ubiquinone oxidoreductase from bovine heart mitochondria. Complementary DNA sequence of the import precursor of the 10 kDa subunit of the flavoprotein fragment. FEBS Lett. 282, 135138.
Smith W. W., Pattridge K. A. & Ludwig M. L. (1983). Structure of oxidised flavodoxin from Anacystis nidulans. J. molec. Biol. 165, 737755.
Srivastava D. K. & Bernhard S. A. (1986). Metabolite transfer via enzyme-enzyme complexes. Science 234, 10811086.
Steinmetz A. A., Castroviejo M., Sayre R. T. & Bogorad L. (1986). Protein PSIIG. An additional component of photosystem II identified through its plastic gene in maize. J. biol. Chem. 261, 24852488.
Steinmuller K., Ley A. C., Steinmetz A. A., Sayre R. T. & Bogorad L. (1989). Characterization of the ndhC-psbG-ORF 157/159 operon of maize plastid DNA and of the cyanobacterium Synechocystis sp. PCC6803. Mol. Gen. Genet. 216, 6069.
Stern D. B., Bang A. G. & Thompson W. F. (1986). The watermelon mitochondrial URF-i structure: evidence for a complex structure. Curr. Genet. 10, 857869.
Sugiyama S., Hattori K., Hayakawa M. & Ozawa T. (1991). Quantitative analysis of age-associated accumulation of mitochondrial DNA with deletion in human hearts. Biochem. biophys. Res. Commun. 180, 894899.
Sumegi B. & Srere P. A. (1984). Complex I binds several mitochondrial NADcoupled dehydrogenases. J. biol. Chem. 259, 1504015045.
Suzuki H. & King T. (1983). Evidence of an ubisemiquinone radical(s) from the NADH-ubiquinone reductase of the mitochondrial respiratory chain. J. biol. Chem. 258, 352358.
Suzuki H. & Ozawa T. (1986). An ubiquinone-binding protein in mitochondrial NADH-ubiquinone reductase (complex I). Biochem. biophys. Res. Commun. 138, 12371242.
Suzuki T., Kazama S., Hirai A., Akihama T. & Kadowaki K. (1991). The rice mitochondrial nadj gene has an extended reading frame at its 5 end: nucleotide sequence analysis of rice trnS, nadj, and rpsi2 genes. Curr. Genet. 20, 331337.
Taketani S., Tanaka-Yoshioka A., Masaki R., Tashiro Y. & Tokunaga R. (1986). Association of ferrochelatase with complex I in bovine heart mitochondria. Biochim. biophys. Acta 883, 277283.
Taketani S., Nakahashi Y., Osumi T. & Tokunaga R. (1990). Molecular cloning, sequencing, and expression of mouse ferrochelatase. J. biol. Chem. 265, 1937719380.
Taylor S. S. (1977). Amino acid sequence of dogfish muscle lactate dehydrogenase. J.biol. Chem. 252, 17991806.
Thomson A. J. (1991). Does ferredoxin (Azotobacter) represent a novel class of DNA binding proteins that regulate gene expression in response to cellular iron (II)? FEBS Lett. 285, 230236.
Towler D. A., Adams S. P., Eubanks S. R., Towery D. S., Jackson-Machelski E., Glaser L. & Gordon J. I. (1988). Myristoyl CoA:protein. N-myristoyltransferase activities from rat liver and yeast possess overlapping yet distinct peptide substrate specificies. J. biol. Chem. 263, 17841790.
Tran-Betcke A., Warnecke U., Bocker C., Zabarosch C. & Friedrich B. (1990). Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H 16. J. Bacteriol. 172, 29202929.
Trounce I., Byrne R. & Marzuki S. (1989). Decline in human skeletal muscle mitochondrial respiratory chain function: possible factor in ageing. Lancet i, 637639.
Trumpower B. L. (1990). The protonmotive Q cycle. J. biol. Chem. 265, 1140911412.
Tuschen G., Sackmann U., Nehls U., Haiker H., Buse G. & Weiss H. (1990). Assembly of NADH:ubiquinone reductase (complex I) in Neurospora mitochondria: independent pathways of nuclear encoded and mitochondrially encoded subunits. J. molec. Biol. 213, 845857.
Unemoto T. & Hayashi M. (1989). Sodium transport NADH-quinone reductase of a marine Vibrio alginolyticus. J. Bioenerget. Biomembr. 21, 649662.
Van Belzen R., Van Gaalen M. C. M., Cupyers P. A. & Albracht S. P. J. (1990). New evidence for the dimeric nature of NADH: Q oxidoreductase in bovine heart submitochondrial particles. Biochim. biophys. Acta 1017, 152159.
Van Belzen R., De Jong A. M. P. & Albracht S. J. P. (1992). On the stoichiometry of the iron-sulphur clusters in mitochondrial NADH: Q oxidoreductase. Eur. J. Biochem. (submitted).
Van Der Pas J. C., Rohlen D. A., Weidner U. & Weiss H. (1991). Primary structure of the nuclear encoded 29–9 kDa subunit of NADH:ubiquinone reductase from Neurospora crassa mitochondria. Biochim. biophys. Acta 1089, 389390.
Vanaman T. C., Wakil S. J. & Hill R. L. (1968). The complete amino acid sequence of the acyl carrier protein of Escherichia coli. J. biol. Chem. 243, 6420–6231.
Vercesi A., Reynafarje B. & Lehninger A. L. (1978). Stoichiometry of H+ ejection and Ca2+ uptake coupled to electron transport in rat heart mitochondria. J. biol. Chem. 253, 63796385.
Videira A., Tropschüg M. & Werner S. (1990 a). Primary structure, in vitro expression and import into mitochondria of a 29/21 kDa subunit of complex I from Neurospora crassa. Biochem. biophys. Res. Commun. 166, 280.
Videira A., Tropschüg M., Wachter E., Schneider H. & Werner S. (1990 b). Molecular cloning of subunits of complex I from Neurospora crassa Primary structure and in vitro expression of a 22 kDa polypeptide. J. biol. Chem. 265, 1306013065.
Videira A., Tropschüg M. & Werner S. (1990 c). Primary structure and expression of a nuclear-encoded subunit of complex I homologous to proteins specified by the chloroplast genome. Biochem. biophys. Res. Commun. 171, 11681174.
Von Bahr-Lindström H., Galante Y. M., Persson M. & Jornvall H. (1983). The primary structure of subunit II of NADH dehydrogenase from bovine heart mitochondria. Eur. J. Biochem. 134, 145150.
Vuokila P. T. & Hassinen I. E. (1988). N,N′-dicyclohexylcarbodiimide sensitivity of bovine heart mitochondrial NADH:ubiquinone oxidoreductase. Biochem J. 249, 339344.
Vuokila P. T. & Hassinen I. E. (1989). DCCD sensitivity of electron and proton transfer by NADH:ubiquinone oxidoreductase in bovine heart submitochondrial particles - a thermodynamic approach. Biochim. biophys. Acta 974, 219222.
Walker J. E. & Cozens A. L. (1986). Evolution of ATP synthase. Chemica Scripta 26B, 263272.
Walker J. E., Saraste M. & Gay N. J. (1984). The unc operon: nucleotide sequence, regulation and structure of ATP synthase. Biochim. Biophys. Acta 768, 164200.
Walker J. E., Lutter R., Dupuis A. & Runswick M. J. (1991). Identification of the subunits of F1 F0-ATPase from bovine heart mitochondria. Biochemistry 30, 53695378.
Walker J. E., Arizmendi J. M., Dupuis A., Fearnley I. M., Finel M., Medd S. M., Pilkington S. J., Runswick M. J. & Skehel J. M. (1992). Sequences of twenty subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction. J. molec. Biol. (in the press).
Wallace D. C. (1989). Mitochondrial DNA mutations and neuromuscular disease. Trends in Genetics 5, 913.
Wallace D. C. (1992). Mitochondrial genetics: a paradigm for ageing and degenerative diseases? Science 256, 628632.
Wallace D. C., Singh G., Lott M. T., Hodge J. A., Schurr T. G., Lezza A. M. S., Elsas L. J. & Nikoskelainen (1988). Mitochondrial DNA mutation associated with Leber's hereditary optic neuropathy. Science 242, 14271430.
Wang D. C., Meinhardt S. W., Sackmann U., Weiss H. & Ohnishi T. (1991). The iron–sulfur clusters in the two related forms of mitochondrial NADH:ubiquinone oxidoreductase made by Neurospora crassa. Eur. J. Biochem. 197, 257264.
Weidner U., Sackmann U., Nehls U. & Weiss H. (1991). Primary structure of the nuclear encoded 18–3 kDa subunit of NADH:ubiquinone reductase (complex I) from Neurospora crassa mitochondria. Biochim. biophys. Acta 1089, 391392.
Weiss H. & Friedrich T. (1991). Redox linked proton translocation by NADHubiquinone reductase (complex I). J. Bioenerget. Biomembr. 23, 743754.
Weiss H., Friedrich T., Hofhaus G. & Preis D. (1991). The respiratory chain NADH dehydrogenase (complex I) of mitochondria. Eur. J. Biochem. 197, 563576.
White J. L., Hackert M. L., Buehner M., Adams M. J., Ford G. C., Lentz P. J. Jr, Smiley I. E., Steindel S. J. & Rossmann M. G. (1976). A comparison of the structures of apo dogfish M4 lactate dehydrogenase and its ternary complexes. J. molec. Biol. 102, 759779.
Wierenga R. K., Terpstra P. & Hol W. G. J. (1986). Prediction of the occurrence of the ADP-binding bab-fold in proteins, using an amino acid sequence fingerprint. J. molec. Biol. 187, 101107.
Wikström M. (1984). Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone. FEBS Lett. 169, 300304.
Willeford K. O., Gomobos Z. & Gibbs M. (1989). Evidence for chloroplastic succinate dehydrogenase participating in the chloroplastic respiratory and photosynthetic electron transport chains of Chlamydomonas reinhardtii. Plant Physiol. 90, 10841087.
Wintz H., Chen H. C. & Pillay D. T. N. (1989). Partial characterization of the gene coding for subunit IV of soybean mitochondrial NADH dehydrogenase. Curr. Genet. 15, 155160.
Wittmann H. G. (1982). Components of bacterial ribosomes. Ann. Rev. Biochem. 51, 155183.
Wu M., Nie Z. Q. & Yang J. (1989). The 18 kDa protein that binds to the chloroplast DNA replicative organ is an iron-sulfur protein related to a subunit of NADH dehydrogenase. Plant Cell 1, 551557.
Xia Z. X. & Mathews F. S. (1990). Molecular structure of flavocytochrome b2 at 2°4 Å resolution. J. molec. Biol. 212, 837863.
Xu X., Matsuno-Yagi A. & Yagi T. (1991 a). The NADH binding subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: gene cloning and deduced primary structure. Biochemistry 30, 64226428.
Xu X., Matsuno-Yagi A. & Yagi T. (1991 b). Characterization of the 25 kilodalton subunit of the energy transducing NADH-ubiquinone oxidoreductase (NDH-I) of Paracoccus denitrificans: sequence similarity to the 24 kilodalton subunit of the flavoprotein fraction of mammalian complex I. Biochemistry 30, 86788684.
Yagi T. (1986). Purification and characterization of NADH dehydrogenase complex from Paracoccus denitrificans. Arch. Biochem. Biophys. 250, 302311.
Yagi T. (1987). Inhibition of NADH-ubiquinone reductase activity by N, N′ -dicyclohexylcarbodiimide and correlation of this inhibition with the occurrence of energy-coupling site I in various organisms. Biochemistry 26, 28222828.
Yagi T. (1990). Inhibition by capsaicin of NADH-quinone oxidoreductases is correlated with the presence of energy-coupling site 1 in various organisms. Arch. Biochem. Biophys. 281, 305311.
Yagi T. (1991). Bacterial NADH-quinone oxidoreductases. J. Bioenerget. Biontembr. 23, 211225.
Yagi T. & Dinh T. M. (1990). Identification of the NADH-binding subunit of NADH-ubiquinone oxidoreductase of Paracoccus denitrificans. Biochemistry 29, 5515552O.
Yagi T. & Hatefi Y. (1988). Identification of the dicyclohexylcarbodiimide binding subunit of NADH-ubiquinone oxidoreductase (complex I). J. biol. Chem. 263, 1615016155.
Yagi T., Hon-Nami K. & Ohnishi T. (1988). Purification and characterisation of two types of NADH-quinone reductase from Thermus thermophilus HB-8. Biochemistry 27, 20082013.
Yagi T., Xu X. & Matsuno-Yagi A. (1991). Gene cluster of the energy transducing NADH-ubiquinone oxidoreductase (NDH-I) of Paracoccus denitrificans. Biol. Chem. Hoppe-Seyler 372, 555.
Yamomoto H., Tanaka M., Katayama M., Obayashi T., Nimura Y. & Ozawa T. (1992). Significant existence of deleted mitochondrial DNA in cirrhotic liver surrounding hepatic tumor. Biochem. biophys. Res. Commun. 182, 913920.
Yang X. & Trumpower B. L. (1986). Purification of a three subunit ubiquinolcytochrome c oxidoreductase complex from Paracoccus denitrificans. J. biol. Chem. 261, 1228212289.
Yeaman S. J., Fussey S. P. M., Danner D. J., James O. F. W., Mutimer D. J. & Bassendine M. F. (1988). Primary biliary cirrhosis: identification of two major M2 mitochondrial autoantigens. Lancet i, 10671070.
Yoshino H., Nakaga-Wahattori Y., Kondo T. & Mizuno Y. (1992). Mitochondrial complex I and complex II activities of lymphocytes and platelets in Parkinson's disease. J. Neural Transm. (Parkinson's Disease Section) 4, 2734.
Young I. G., Rogers B. L., Campbell H. D., Jaworowski A. & Shaw D. C. (1981). Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli. Eur.J. Biochem. 116, 165170.
Zeviani M., Moraes C. T., Dimauro S., Nakase H., Bonilla E., Schon E. A. & Rowland L. P. (1988). Deletions of mitochondrial DNA in Kearns-Sayre syndrome. Neurology 38, 13391346.
Zeviani M., Servidei S., Gellera C., Bertini E., Dimauro S. & Didonato S. (1989). An autosomal dominant disorder with multiple deletions of mitochondrial DNA starting at the D-loop region. Nature 339, 309311.
Zhao H.-F, Simard J., Labrie C., Breton N., Rheaume E., Lue-The V. & Labrie F. (1989). Molecular cloning, cDNA structure and predicted amino acid sequence of bovine 3β-hydroxy-5-ene steroid dehydrogenase/Δ54 isomerase. FEBS Lett. 259, 153157.
Zhu D., Economu E. P., Antonarakis S. E. & Maumenee I. H. (1992). Mitochondrial DNA mutation and heteroplasmy in type I Leber optic neuropathy. Am. J. Med. Genet. 42, 173179.
Recommend this journal

Email your librarian or administrator to recommend adding this journal to your organisation's collection.

Quarterly Reviews of Biophysics
  • ISSN: 0033-5835
  • EISSN: 1469-8994
  • URL: /core/journals/quarterly-reviews-of-biophysics
Please enter your name
Please enter a valid email address
Who would you like to send this to? *


Full text views

Total number of HTML views: 0
Total number of PDF views: 54 *
Loading metrics...

Abstract views

Total abstract views: 550 *
Loading metrics...

* Views captured on Cambridge Core between September 2016 - 22nd October 2017. This data will be updated every 24 hours.