Genomes and Genes
Gene Symbol: nuoL
Description: NADH:ubiquinone oxidoreductase, membrane subunit L
Alias: ECK2272, JW2273
Species: Escherichia coli str. K-12 substr. MG1655
- 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. ..
- 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. ..
- 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...
- 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. ..
- Verkhovskaya M, Belevich N, Euro L, Wikstrom M, Verkhovsky M. Real-time electron transfer in respiratory complex I. Proc Natl Acad Sci U S A. 2008;105:3763-7 pubmed publisher..Possible consequences of these findings for the proton translocation mechanism are discussed. ..
- 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..Exchange into decyl maltoside led to the removal of the hydrophobic subunit NuoL from the otherwise intact complex...
- Matsushita K, Ohnishi T, Kaback H. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry. 1987;26:7732-7 pubmed
- 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. ..
- Nakamaru Ogiso E, Kao M, Chen H, Sinha S, Yagi T, Ohnishi T. The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex I. J Biol Chem. 2010;285:39070-8 pubmed publisher..Here, to investigate the proton pumping mechanism by complex I, we focused on the largest transmembrane subunit NuoL (Escherichia coli ND5 homolog)...
- Steimle S, Bajzath C, Dörner K, Schulte M, Bothe V, Friedrich T. Role of subunit NuoL for proton translocation by respiratory complex I. Biochemistry. 2011;50:3386-93 pubmed publisher..The helix corresponds to the C-terminal part of the most distal subunit NuoL. To investigate its role in proton translocation, we characterized the electron transfer and proton translocation ..
- 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..coli complex I. A partially assembled complex I bound to the membrane was detected in the nuoK and nuoL mutants, respectively...
- 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. ..
- 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. ..
- 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. ..
- Pohl T, Uhlmann M, Kaufenstein M, Friedrich T. Lambda Red-mediated mutagenesis and efficient large scale affinity purification of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Biochemistry. 2007;46:10694-702 pubmed..After reconstitution in proteoliposomes it couples the electron transfer with proton translocation in an inhibitor sensitive manner, thus meeting all prerequisites for structural and functional studies. ..
- 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. ..
- Satoh T, Miyoshi H, Sakamoto K, Iwamura H. Comparison of the inhibitory action of synthetic capsaicin analogues with various NADH-ubiquinone oxidoreductases. Biochim Biophys Acta. 1996;1273:21-30 pubmed..1990) Arch. Biochem. Biophys. 281, 305-311). It is noteworthy that several synthetic capsaicins discriminated between NDH-1 and NDH-2 much better than natural capsaicin. ..
- 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. ..
- 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. ..
- 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...
- 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. ..
- 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. ..
- 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. ..
- 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
- 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. ..
- 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. ..
- Michel J, DeLeon Rangel J, Zhu S, Van Ree K, Vik S. Mutagenesis of the L, M, and N subunits of Complex I from Escherichia coli indicates a common role in function. PLoS ONE. 2011;6:e17420 pubmed publisher..The results show a close correlation with reduced activity among the corresponding mutations, and provide evidence that the L, M, and N subunits have a common role in Complex I. ..
- 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. ..
- 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. ..
- Poole R, Haddock B. Energy-linked reduction of nicotinamide--adenine dinucleotide in membranes derived from normal and various respiratory-deficient mutant strains of Escherichia coli K12. Biochem J. 1974;144:77-85 pubmed..8. Results are interpreted as evidence of the ubiquinone-dependent, but cytochrome-independent, nature of the site I region of the respiratory chain in E. coli. ..
- Hellwig P, Scheide D, Bungert S, Mäntele W, Friedrich T. FT-IR spectroscopic characterization of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli: oxidation of FeS cluster N2 is coupled with the protonation of an aspartate or glutamate side chain. Biochemistry. 2000;39:10884-91 pubmed..Part of these signals are attributed to the reorganization of protonated/deprotonated Asp or Glu side chains. On the basis of these data we discuss the role of N2 for proton translocation of complex I. ..
- 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. ..
- Narayanan M, Sakyiama J, Elguindy M, Nakamaru Ogiso E. Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. J Biochem. 2016;160:205-215 pubmed..Here, to gain mechanistic insights into the role of subunit NuoL, we investigated the effects of Mg2+, Zn2+ and the Na+/H+ antiporter ..
- 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. ..
- 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. ..
- Uhlmann M, Friedrich T. EPR signals assigned to Fe/S cluster N1c of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) derive from cluster N1a. Biochemistry. 2005;44:1653-8 pubmed..Thus, there is no third binuclear iron-sulfur "N1c" in the E. coli complex I but an additional tetranuclear cluster that may be coined N7. ..
- 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. ..
- 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. ..
- Steimle S, Willistein M, Hegger P, Janoschke M, Erhardt H, Friedrich T. Asp563 of the horizontal helix of subunit NuoL is involved in proton translocation by the respiratory complex I. FEBS Lett. 2012;586:699-704 pubmed publisher..It is discussed that this residue is involved in transferring protons to the membranous proton translocation site. ..
- 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. ..
- Friedrich T, Stolpe S, Schneider D, Barquera B, Hellwig P. Ion translocation by the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Biochem Soc Trans. 2005;33:836-9 pubmed..We did not find any indications for Na+ translocation by the E. coli complex I. ..
- 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
- Yagi T. Inhibition by capsaicin of NADH-quinone oxidoreductases is correlated with the presence of energy-coupling site 1 in various organisms. Arch Biochem Biophys. 1990;281:305-11 pubmed..The mechanism by which capsaicin inhibits the energy-transducing NADH-quinone oxidoreductase is discussed. ..
- 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..Expression of a C-terminally truncated version of the hydrophobic NuoL subunit (ND5 homologue) from E. coli complex I resulted in Na+-dependent growth inhibition of the E...
- Kaila V, Wikstr m M, Hummer G. Electrostatics, hydration, and proton transfer dynamics in the membrane domain of respiratory complex I. Proc Natl Acad Sci U S A. 2014;111:6988-93 pubmed publisher..explore the functional relevance of the pseudosymmetric inverted-repeat structures of the antiporter-like subunits NuoL/M/N, we constructed a symmetry-related structure of a possible alternate-access state...
- Zhu S, Vik S. Constraining the Lateral Helix of Respiratory Complex I by Cross-linking Does Not Impair Enzyme Activity or Proton Translocation. J Biol Chem. 2015;290:20761-73 pubmed publisher..One of the integral membrane subunits, nuoL in Escherichia coli, has an unusual lateral helix of âˆ¼75 residues that lies parallel to the membrane surface ..
- 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. ..
- Baranova E, Morgan D, Sazanov L. Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex I. J Struct Biol. 2007;159:238-42 pubmed..The membrane domain of the complex contains three similar antiporter-like subunits NuoL/M/N, probably involved in proton pumping...
- Nakashima K, Sugiura A, Kanamaru K, Mizuno T. Signal transduction between the two regulatory components involved in the regulation of the kdpABC operon in Escherichia coli: phosphorylation-dependent functioning of the positive regulator, KdpE. Mol Microbiol. 1993;7:109-16 pubmed
- Steuber J. The Na+-translocating NADH:quinone oxidoreductase (NDH I) from Klebsiella pneumoniae and Escherichia coli: implications for the mechanism of redox-driven cation translocation by complex I. J Bioenerg Biomembr. 2001;33:179-86 pubmed..Special attention is given to the membranous NuoL (ND5, Nqo12) subunits that possess striking sequence similarities to secondary Na+/H+ antiporters and are proposed ..
- Esterházy D, King M, Yakovlev G, Hirst J. Production of reactive oxygen species by complex I (NADH:ubiquinone oxidoreductase) from Escherichia coli and comparison to the enzyme from mitochondria. Biochemistry. 2008;47:3964-71 pubmed publisher..In contrast, bovine complex I produces 95% superoxide. The results are consistent with (but do not prove) a specific role for cluster N1a in determining the outcome of O2 reduction; possible reaction mechanisms are discussed. ..
- Finel M, Majander A. Studies on the proton-translocating NADH:ubiquinone oxidoreductases of mitochondria and Escherichia coli using the inhibitor 1,10-phenanthroline. FEBS Lett. 1994;339:142-6 pubmed..EPR spectroscopy of membranous E. coli NDH1 shows that two slow- and one fast-relaxing Fe-S clusters become detectable upon reduction by NADH in the presence of OP. However, none of them resembles the mitochondrial cluster 2. ..
- 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. ..
- 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. ..
- 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..To elucidate the mechanism of Na(+) transport, the C-terminally truncated NuoL subunit (NuoL(N)) which is related to Na(+)/H(+) antiporters was expressed as a protein A fusion protein (ProtA-..
- Belevich G, Knuuti J, Verkhovsky M, Wikstrom M, Verkhovskaya M. Probing the mechanistic role of the long ?-helix in subunit L of respiratory Complex I from Escherichia coli by site-directed mutagenesis. Mol Microbiol. 2011;82:1086-95 pubmed publisherThe C-terminus of the NuoL subunit of Complex I includes a long amphipathic ?-helix positioned parallel to the membrane, which has been considered to function as a piston in the proton pumping machinery...
- Yagi T, Matsuno Yagi A. The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked. Biochemistry. 2003;42:2266-74 pubmed
- 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. ..
- 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. ..
- 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. ..
- 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
- 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. ..
- Mamedova A, Holt P, Carroll J, Sazanov L. Substrate-induced conformational change in bacterial complex I. J Biol Chem. 2004;279:23830-6 pubmed..The enzyme retains its L-shape in the presence of NADH, but exhibits a significantly more open or expanded structure both in the peripheral arm and, unexpectedly, in the membrane domain also. ..