nuoC

Summary

Gene Symbol: nuoC
Description: NADH:ubiquinone oxidoreductase, fused CD subunit
Alias: ECK2280, JW5375, nuoCD, nuoD
Species: Escherichia coli str. K-12 substr. MG1655
Products:     nuoC

Top Publications

  1. Zarbiv G, Li H, Wolf A, Cecchini G, Caplan S, Sourjik V, et al. Energy complexes are apparently associated with the switch-motor complex of bacterial flagella. J Mol Biol. 2012;416:192-207 pubmed publisher
  2. Friedrich T. Complex I: a chimaera of a redox and conformation-driven proton pump?. J Bioenerg Biomembr. 2001;33:169-77 pubmed
    ..This implies that complex I contains two energy-coupling sites. The NADH dehydrogenase module seems to be involved in electron transfer and not in proton translocation. ..
  3. Amarneh B, De Leon Rangel J, Vik S. Construction of a deletion strain and expression vector for the Escherichia coli NADH:ubiquinone oxidoreductase (Complex I). Biochim Biophys Acta. 2006;1757:1557-60 pubmed
    ..A chromosomal deletion of all nuo genes has been achieved by homologous recombination. A vector that encodes all of the nuo genes has been constructed, and it expresses a functional enzyme. ..
  4. Schneider D, Pohl T, Walter J, Dörner K, Kohlstädt M, Berger A, et al. Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Biochim Biophys Acta. 2008;1777:735-9 pubmed publisher
    ..It is discussed whether this fragment represents an assembly intermediate. In addition, a membrane-bound fragment exhibiting NADH/ferricyanide oxidoreductase activity and containing the iron-sulfur cluster N2 was detected in one mutant. ..
  5. Bungert S, Krafft B, Schlesinger R, Friedrich T. One-step purification of the NADH dehydrogenase fragment of the Escherichia coli complex I by means of Strep-tag affinity chromatography. FEBS Lett. 1999;460:207-11 pubmed
    ..This was achieved by fusing the Strep-tag II peptide to the C-terminus of NuoF or NuoG. Fusion of this peptide to the N-terminus of either NuoE or NuoF disturbed the assembly of the NADH dehydrogenase fragment. ..
  6. Gong X, Xie T, Yu L, Hesterberg M, Scheide D, Friedrich T, et al. The ubiquinone-binding site in NADH:ubiquinone oxidoreductase from Escherichia coli. J Biol Chem. 2003;278:25731-7 pubmed
    ..Using the PHDhtm hydropathy plot, the labeled peptide is located in the transmembrane helix 4 toward the periplasmic side of the membrane. ..
  7. Friedrich T. The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochim Biophys Acta. 1998;1364:134-46 pubmed
  8. Baranova E, Holt P, Sazanov L. Projection structure of the membrane domain of Escherichia coli respiratory complex I at 8 A resolution. J Mol Biol. 2007;366:140-54 pubmed
  9. Zambrano M, Kolter R. Escherichia coli mutants lacking NADH dehydrogenase I have a competitive disadvantage in stationary phase. J Bacteriol. 1993;175:5642-7 pubmed
    ..This is the first identification of genes encoding subunits of NADH dehydrogenase I in E. coli. The significance of the inability of these mutant strains to compete in stationary-phase cultures is discussed. ..

More Information

Publications54

  1. Kao M, Nakamaru Ogiso E, Matsuno Yagi A, Yagi T. Characterization of the membrane domain subunit NuoK (ND4L) of the NADH-quinone oxidoreductase from Escherichia coli. Biochemistry. 2005;44:9545-54 pubmed
    ..Possible roles of these arginine residues and other conserved residues in the NuoK subunit for NDH-1 function were discussed. ..
  2. Kao M, Di Bernardo S, Nakamaru Ogiso E, Miyoshi H, Matsuno Yagi A, Yagi T. Characterization of the membrane domain subunit NuoJ (ND6) of the NADH-quinone oxidoreductase from Escherichia coli by chromosomal DNA manipulation. Biochemistry. 2005;44:3562-71 pubmed
    ..Together with the results on mutations related to human diseases, possible functional roles of the NuoJ subunit have been discussed. ..
  3. Braun M, Bungert S, Friedrich T. Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochemistry. 1998;37:1861-7 pubmed
    ..The preparation fulfills all prerequisites for crystallization of the fragment. ..
  4. Bottcher B, Scheide D, Hesterberg M, Nagel Steger L, Friedrich T. A novel, enzymatically active conformation of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). J Biol Chem. 2002;277:17970-7 pubmed
    ..Only the horseshoe-shaped complex I exhibits enzyme activity in detergent solution, which is abolished by the addition of salt. Therefore, it is proposed that this structure is the native conformation of the complex in the membrane. ..
  5. Archer C, Elliott T. Transcriptional control of the nuo operon which encodes the energy-conserving NADH dehydrogenase of Salmonella typhimurium. J Bacteriol. 1995;177:2335-42 pubmed
    ..Mutations in the global regulatory genes arcA, oxrA (fnr), crp, cya, and katF were tested for effects on expression of the nuo operon. However, none of the mutations tested had a large effect on expression of type I NADH dehydrogenase. ..
  6. Calhoun M, Oden K, Gennis R, de Mattos M, Neijssel O. Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain. J Bacteriol. 1993;175:3020-5 pubmed
  7. Tran Q, Bongaerts J, Vlad D, Unden G. Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in respiration of NADH to fumarate and its bioenergetic implications. Eur J Biochem. 1997;244:155-60 pubmed
    ..NADH-->dimethylsulfoxide respiration is also dependent on NADH dehydrogenase I. The consequences for energy conservation by anaerobic respiration with NADH as a donor are discussed. ..
  8. Leif H, Sled V, Ohnishi T, Weiss H, Friedrich T. Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur J Biochem. 1995;230:538-48 pubmed
    ..This subunit arrangement coincidences to some extent with the order of the genes on the nuo operon. A topological model of the E. coli complex I is proposed...
  9. Holt P, Morgan D, Sazanov L. The location of NuoL and NuoM subunits in the membrane domain of the Escherichia coli complex I: implications for the mechanism of proton pumping. J Biol Chem. 2003;278:43114-20 pubmed
    ..Among the hydrophilic subunits, NuoCD was most readily dissociated from the complex, whereas NuoB was partially dissociated from the peripheral arm ..
  10. Unden G, Bongaerts J. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim Biophys Acta. 1997;1320:217-34 pubmed
    ..Reductive activation could be achieved by cellular reductants in the absence of O2. In addition, O2 may cause destruction and loss of the FeS cluster. It is not known whether this process is required for regulation of FNR function. ..
  11. Pr ss B, Nelms J, Park C, Wolfe A. Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids. J Bacteriol. 1994;176:2143-50 pubmed
    ..We propose that cells defective for NADH dehydrogenase I exhibit all these phenotypes, because large NADH/NAD+ ratios inhibit certain tricarboxylic acid cycle enzymes, e.g., citrate synthase and malate dehydrogenase...
  12. Belevich G, Euro L, Wikstrom M, Verkhovskaya M. Role of the conserved arginine 274 and histidine 224 and 228 residues in the NuoCD subunit of complex I from Escherichia coli. Biochemistry. 2007;46:526-33 pubmed
    The conserved arginine 274 and histidine 224 and 228 residues in subunit NuoCD of complex I from Escherichia coli were substituted for alanine. The wild-type and mutated NuoCD subunit was expressed on a plasmid in an E...
  13. Sazanov L. Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry. 2007;46:2275-88 pubmed
    ..In this review, novel mechanistic implications of the structure are discussed, and the effects of many known mutations of complex I subunits are interpreted in a structural context. ..
  14. Gemperli A, Schaffitzel C, Jakob C, Steuber J. Transport of Na(+) and K (+) by an antiporter-related subunit from the Escherichia coli NADH dehydrogenase I produced in Saccharomyces cerevisiae. Arch Microbiol. 2007;188:509-21 pubmed
    ..The cation selectivity and function of the NuoL subunit as a transporter module of the NADH dehydrogenase complex is discussed. ..
  15. Castro Guerrero N, Sinha P, Torres Bacete J, Matsuno Yagi A, Yagi T. Pivotal roles of three conserved carboxyl residues of the NuoC (30k) segment in the structural integrity of proton-translocating NADH-quinone oxidoreductase from Escherichia coli. Biochemistry. 2010;49:10072-80 pubmed publisher
    ..NDH-1, the hydrophilic subunits NuoC/Nqo5/30k and NuoD/Nqo4/49k are fused together in a single polypeptide as the NuoCD subunit. The NuoCD subunit is the only subunit that does not bear a cofactor in the peripheral arm...
  16. David P, Baumann M, Wikstrom M, Finel M. Interaction of purified NDH-1 from Escherichia coli with ubiquinone analogues. Biochim Biophys Acta. 2002;1553:268-78 pubmed
    ..Both ubiquinone-2 and decylubiquinone are good acceptors for this enzyme, while affinity of NDH-1 for ubiquinone-1 is clearly lower than for the other two, particularly in the purified state. ..
  17. Matsushita K, Ohnishi T, Kaback H. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry. 1987;26:7732-7 pubmed
  18. Hayashi M, Miyoshi T, Takashina S, Unemoto T. Purification of NADH-ferricyanide dehydrogenase and NADH-quinone reductase from Escherichia coli membranes and their roles in the respiratory chain. Biochim Biophys Acta. 1989;977:62-9 pubmed
    ..The FAD-containing NQR was very similar to that purified by Jaworowski et al. (Biochemistry (1981) 20, 2041-2047), and reduced Q1 without generating delta psi. ..
  19. Wackwitz B, Bongaerts J, Goodman S, Unden G. Growth phase-dependent regulation of nuoA-N expression in Escherichia coli K-12 by the Fis protein: upstream binding sites and bioenergetic significance. Mol Gen Genet. 1999;262:876-83 pubmed
    ..This ensures higher ATP yields under conditions where large amounts of ATP are required. ..
  20. Guenebaut V, Schlitt A, Weiss H, Leonard K, Friedrich T. Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I). J Mol Biol. 1998;276:105-12 pubmed
  21. Choice E, Masin D, Bally M, Meloche M, Madden T. Liposomal cyclosporine. Comparison of drug and lipid carrier pharmacokinetics and biodistribution. Transplantation. 1995;60:1006-11 pubmed
  22. Berrisford J, Thompson C, Sazanov L. Chemical and NADH-induced, ROS-dependent, cross-linking between subunits of complex I from Escherichia coli and Thermus thermophilus. Biochemistry. 2008;47:10262-70 pubmed publisher
    ..chemical cross-linker, incubation of complex I with NADH resulted in covalent cross-links between subunits Nqo4 (NuoCD) and Nqo6 (NuoB), as well as between Nqo6 and Nqo9...
  23. Neijssel O, Teixeira de Mattos M. The energetics of bacterial growth: a reassessment. Mol Microbiol. 1994;13:172-82 pubmed
    ..The different strains indeed show different growth efficiencies. The physiological significance of energetically less-efficient branches of the respiratory chain is discussed. ..
  24. Friedrich T, Weidner U, Nehls U, Fecke W, Schneider R, Weiss H. Attempts to define distinct parts of NADH:ubiquinone oxidoreductase (complex I). J Bioenerg Biomembr. 1993;25:331-7 pubmed
    ..This assumption is further supported by the conserved order of bacterial complex I genes, which correlates with the topological arrangement of the corresponding subunits in the two parts of complex I. ..
  25. Mamedova A, Holt P, Carroll J, Sazanov L. Substrate-induced conformational change in bacterial complex I. J Biol Chem. 2004;279:23830-6 pubmed
    ..prevented the formation of cross-links between the hydrophilic subunits of the complex, including NuoB, NuoI, and NuoCD. Comparisons using different cross-linkers suggested that NuoB, which is likely to coordinate the key iron-sulfur ..
  26. Sinegina L, Wikstrom M, Verkhovsky M, Verkhovskaya M. Activation of isolated NADH:ubiquinone reductase I (complex I) from Escherichia coli by detergent and phospholipids. Recovery of ubiquinone reductase activity and changes in EPR signals of iron-sulfur clusters. Biochemistry. 2005;44:8500-6 pubmed
    ..895, 1.904, 2.05, which corresponds to the parameters reported for the N2 cluster. This data indicates conformational rearrangements of catalytic importance in complex I upon binding of phospholipids. ..
  27. Calhoun M, Gennis R. Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli. J Bacteriol. 1993;175:3013-9 pubmed
    ..The enzyme encoded by this locus probably translocates protons across the inner membrane, contributing to the proton motive force. ..
  28. Steuber J, Schmid C, Rufibach M, Dimroth P. Na+ translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli. Mol Microbiol. 2000;35:428-34 pubmed
    ..With an E. coli mutant deficient in complex I, the Na+ transport activity was low (1-3 nmol mg-1 min-1), and rotenone was without effect. ..
  29. Friedrich T, Scheide D. The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases. FEBS Lett. 2000;479:1-5 pubmed
    ..Six of them are also present in a family of membrane-bound multisubunit [NiFe] hydrogenases. It is discussed that they build a module for electron transfer coupled to proton translocation. ..
  30. Yang Y, Bennett G, San K. Effect of inactivation of nuo and ackA-pta on redistribution of metabolic fluxes in Escherichia coli. Biotechnol Bioeng. 1999;65:291-7 pubmed
    ..Mutations in both ackA-pta and nuo are required to significantly reduce the flux through the PFL pathway. ..
  31. Yagi T, Matsuno Yagi A. The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked. Biochemistry. 2003;42:2266-74 pubmed
  32. Erhardt H, Steimle S, Muders V, Pohl T, Walter J, Friedrich T. Disruption of individual nuo-genes leads to the formation of partially assembled NADH:ubiquinone oxidoreductase (complex I) in Escherichia coli. Biochim Biophys Acta. 2012;1817:863-71 pubmed publisher
    ..The inactive population is missing cluster N2 and is tightly associated with the inducible lysine decarboxylase. This article is part of a Special Issue entitled: Biogenesis/Assembly of Respiratory Enzyme Complexes. ..
  33. Torres Bacete J, Nakamaru Ogiso E, Matsuno Yagi A, Yagi T. Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1: conserved charged residues essential for energy-coupled activities. J Biol Chem. 2007;282:36914-22 pubmed
    ..The data suggest that these His are not involved in the catalytic Q-binding. Functional roles of NuoM and advantages of NDH-1 research as a model for mitochondrial complex I study have been discussed. ..
  34. Leif H, Weidner U, Berger A, Spehr V, Braun M, van Heek P, et al. Escherichia coli NADH dehydrogenase I, a minimal form of the mitochondrial complex I. Biochem Soc Trans. 1993;21:998-1001 pubmed
  35. Steuber J. The C-terminally truncated NuoL subunit (ND5 homologue) of the Na+-dependent complex I from Escherichia coli transports Na+. J Biol Chem. 2003;278:26817-22 pubmed
    ..This Na+ uptake was prevented by EIPA (5-(N-ethyl-N-isopropyl)-amiloride), which acts as inhibitor against Na+/H+ antiporters. ..
  36. Bogachev A, Murtazina R, Skulachev V. H+/e- stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells. J Bacteriol. 1996;178:6233-7 pubmed
    ..These data suggest that (i) the H+/e- stoichiometry for E. coli NDH-I is at least 1.5 and (ii) the DMSO reductase does not generate a proton motive force. ..
  37. Kervinen M, Pätsi J, Finel M, Hassinen I. A pair of membrane-embedded acidic residues in the NuoK subunit of Escherichia coli NDH-1, a counterpart of the ND4L subunit of the mitochondrial complex I, are required for high ubiquinone reductase activity. Biochemistry. 2004;43:773-81 pubmed
  38. Falk Krzesinski H, Wolfe A. Genetic analysis of the nuo locus, which encodes the proton-translocating NADH dehydrogenase in Escherichia coli. J Bacteriol. 1998;180:1174-84 pubmed
    ..In particular, we present evidence that NuoG, a peripheral subunit, is essential for complex I function and that it plays a role in the regulation of nuo expression and/or the assembly of complex I. ..
  39. Friedrich T, Bottcher B. The gross structure of the respiratory complex I: a Lego System. Biochim Biophys Acta. 2004;1608:1-9 pubmed
    ..This model reflects the evolution of complex I from pre-existing modules for electron transfer and proton translocation. ..
  40. Ohnishi T. Iron-sulfur clusters/semiquinones in complex I. Biochim Biophys Acta. 1998;1364:186-206 pubmed
    ..A brief introduction of EPR technique was also described in Appendix A of this mini-review. ..
  41. Stolpe S, Friedrich T. The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton pump but may be capable of secondary sodium antiport. J Biol Chem. 2004;279:18377-83 pubmed
    ..coli complex I is a primary electrogenic proton pump. However, the magnitude of the pH gradient depended on the sodium concentration. The capability of complex I for secondary Na(+)/H(+) antiport is discussed. ..
  42. Weidner U, Geier S, Ptock A, Friedrich T, Leif H, Weiss H. The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I. J Mol Biol. 1993;233:109-22 pubmed publisher
    ..To some extent, the gene order correlates with the topological arrangement of the encoded subunits. The conception of modular evolution of NADH: ubiquinone oxidoreductase is further supported by the arrangement of the nuo-genes...
  43. Bongaerts J, Zoske S, Weidner U, Unden G. Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-N) of Escherichia coli by electron acceptors, electron donors and gene regulators. Mol Microbiol. 1995;16:521-34 pubmed
    ..A physiological role for the transcriptional stimulation by O2 and nitrate is suggested. ..
  44. Morgan D, Sazanov L. Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides. Biochim Biophys Acta. 2008;1777:711-8 pubmed publisher
    ..The model of the entire bacterial complex I could be built from the crystal structures of subcomplexes using the EM envelope described here. ..
  45. Spehr V, Schlitt A, Scheide D, Guenebaut V, Friedrich T. Overexpression of the Escherichia coli nuo-operon and isolation of the overproduced NADH:ubiquinone oxidoreductase (complex I). Biochemistry. 1999;38:16261-7 pubmed
    ..Due to its stability over a wide pH range and at very high salt concentrations, this preparation is well suited for structural investigations. ..