Escherichia coli K-12 substr. MG1655 Polypeptide: NADH:ubiquinone oxidoreductase, membrane subunit J

Gene: nuoJ Accession Numbers: EG12090 (EcoCyc), b2280, ECK2274

Regulation Summary Diagram: ?

Regulation summary diagram for nuoJ

Component of: NADH:quinone oxidoreductase I (extended summary available)

NuoJ is part of the inner membrane component of NADH dehydrogenase I [Leif95]. The protein has five predicted transmembrane domains; the C terminus is located in the cytoplasm [Daley05]. A crystal structure of the membrane component at higher resolution has allowed better identification of the interactions between the subunits [Efremov11].

Point mutations at conserved residues have been analyzed; mutation of Val65, which is located in the most conserved transmembrane segment, causes significant reduction of coupled electron transfer activity [Kao05a]. Among other site-directed mutants, a V65G mutation had the most deleterious effect on growth on malate and on enzymatic activity [Patsi08].

In the presence of NADH, crosslinking between NuoA and NuoJ in the intact Complex I is abolished, indicating that the conformational change involving the hydrophilic subunits in the presence of NADH extends to the membrane domain [Berrisford08].

Null mutants of all individual nuo genes have a growth defect under aerobic conditions in rich medium [Erhardt12].

nuoJ is one of a network of genes believed to play a role in promoting the stress-induced mutagenesis (SIM) response of E. coli K-12 [Al12].

NuoJ: "NADH:ubiquinone oxidoreductase" [Calhoun93a]

Gene Citations: [Weidner93, Bongaerts95, FalkKrzesinski98, Archer95, Choice95]

Locations: inner membrane

Map Position: [2,393,364 <- 2,393,918] (51.58 centisomes, 186°)
Length: 555 bp / 184 aa

Molecular Weight of Polypeptide: 19.875 kD (from nucleotide sequence)

pI: 5.77

Unification Links: ASAP:ABE-0007536 , CGSC:32652 , DIP:DIP-59258N , EchoBASE:EB2014 , EcoGene:EG12090 , EcoliWiki:b2280 , OU-Microarray:b2280 , PortEco:nuoJ , PR:PRO_000023437 , Protein Model Portal:P0AFE0 , RefSeq:NP_416783 , RegulonDB:EG12090 , SMR:P0AFE0 , String:511145.b2280 , UniProt:P0AFE0

Relationship Links: InterPro:IN-FAMILY:IPR001457 , Pfam:IN-FAMILY:PF00499

In Paralogous Gene Group: 402 (2 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for nuoJ

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred from experiment Inferred by computational analysis [GOA01a, Kao05a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0048038 - quinone binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, Daley05, Leif95]
GO:0005887 - integral component of plasma membrane Inferred from experiment [Daley05]
GO:0030964 - NADH dehydrogenase complex Inferred from experiment [Leif95]
GO:0045272 - plasma membrane respiratory chain complex I Inferred from experiment [Erhardt12, Pohl07a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
metabolism energy metabolism, carbon aerobic respiration
metabolism energy metabolism, carbon anaerobic respiration
metabolism energy production/transport electron donors
transport Primary Active Transporters Oxidoreduction-driven Active Transporters

Essentiality data for nuoJ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Last-Curated ? 01-Dec-2011 by Keseler I , SRI International

Subunit of: NADH:quinone oxidoreductase I

Synonyms: NDH-1, NADH dhI, complex I, NADH dehydrogenase I

Subunit composition of NADH:quinone oxidoreductase I = [NuoA][NuoH][NuoJ][NuoK][NuoL][NuoM][NuoN][(NuoE)(NuoF)(NuoG)][(NuoB)(NuoC)(NuoI)]
         NADH:ubiquinone oxidoreductase, membrane subunit A = NuoA (extended summary available)
         NADH:ubiquinone oxidoreductase, membrane subunit H = NuoH (extended summary available)
         NADH:ubiquinone oxidoreductase, membrane subunit J = NuoJ (extended summary available)
         NADH:ubiquinone oxidoreductase, membrane subunit K = NuoK (extended summary available)
         NADH:ubiquinone oxidoreductase, membrane subunit L = NuoL (extended summary available)
         NADH:ubiquinone oxidoreductase, membrane subunit M = NuoM (extended summary available)
         NADH:ubiquinone oxidoreductase, membrane subunit N = NuoN (extended summary available)
         soluble NADH dehydrogenase fragment = (NuoE)(NuoF)(NuoG) (summary available)
                 NADH:ubiquinone oxidoreductase, chain E = NuoE (summary available)
                 NADH:ubiquinone oxidoreductase, chain F = NuoF (extended summary available)
                 NADH:ubiquinone oxidoreductase, chain G = NuoG (extended summary available)
         connecting fragment of NADH dehydrogenase I = (NuoB)(NuoC)(NuoI) (summary available)
                 NADH:ubiquinone oxidoreductase, chain B = NuoB (extended summary available)
                 NADH:ubiquinone oxidoreductase, chain CD = NuoC (extended summary available)
                 NADH:ubiquinone oxidoreductase, chain I = NuoI (extended summary available)

NADH:ubiquinone oxidoreductase I (NDH-1) is an NADH dehydrogenase that catalyzes the transfer of electrons from NADH to the quinone pool in the cytoplasmic membrane and is able to generate a proton electrochemical gradient. It is part of both the aerobic and anaerobic respiratory chain of the cell. The study of this enzyme is of great interest, because it is considered to be a structurally minimal form of a proton-pumping NADH:ubiquinone oxidoreductase and serves as a model for the more complex mitochondrial enzyme.

NDH-1 is one of two distinct NADH dehydrogenases in E. coli. In contrast to NDH-2 (encoded by ndh), NDH-1-catalyzed electron flow from NADH to ubiquinone generates an electrochemical gradient. Depending on the strain, NDH-2 utilizes NADH exclusively, while NDH-1 can utilize both NADH and d-NADH, which enables specific assays of the enzyme [Matsushita87, Hayashi89, Calhoun93a]

Crystal structures of the membrane domain of NDH-1 have been solved at 3.9 Å resolution [Efremov10] and later at 3 Å resolution [Efremov11]. A plausible mechanism of electron transfer and its coupling to proton translocation has been deduced from this crystal structure and that of the Thermus thermophilus enzyme [Sazanov07, Efremov10]. Proton translocation may be induced by movement of the long amphipathic α-helix of the NuoL subunit that is aligned parallel to the membrane [Efremov10]. This model is discussed in a comment by [Ohnishi10]. The exact number of protons translocated across the membrane remains unknown; the H+/e- stoichiometry is at least 1.5 [Bogachev96]. Recent experiments argue for at least two coupling sites for proton translocation, with NuoL being essential for the translocation of 2H+/2e- [Steimle11]. A crystal structure of the membrane component at higher resolution has allowed identification of possible proton translocation pathways and argues for a purely conformation-driven pathway of proton translocation [Efremov11]. Zn2+ inhibits Ndh-1, possibly by blocking the entry or exit of a proton translocation pathway [Schulte14].

Based on a stoichiometry of 4 H+ translocated per NADH oxidized (2e-), a mixed model for proton translocation using both direct (redox-driven) and indirect (conformation-driven) mechanisms for proton pumping has been presented [Treberg11]. However, a lower ratio of 3H+/2e- has recently been proposed [Wikstrom12]. The Ndh-1 catalytic cycle has been followed in real time, revealing an essentially biphasic reaction [Belevich14].

The purified enzyme can be separated into three components: a soluble fragment composed of the NuoE, F and G subunits which catalyzes the oxidation of NADH, representing the electron input part of the enzyme [Braun98]; an amphipathic connecting fragment composed of the NuoB, CD and I subunits; and a hydrophobic membrane fragment composed of the NuoA, H, J, K, L, M and N subunits [Leif95]. The soluble subunits contain all iron-sulfur clusters and the FMN cofactor; the redox properties of those cofactors have been studied [Euro08], and their intrinsic redox potential was modeled [Medvedev10]. Electron transfer from NADH via FMN to the iron-sulfur centers has been measured in real time [Verkhovskaya08]. Results from crosslinking analysis suggest that the ubiquinone-binding site of the enzyme is located on the membrane subunit NuoM [Gong03], but it has also been modeled to the interface between NuoB and NuoCD based on its location in the T. thermophilus enzyme [Baranova07a]. Site-directed spin labeling is being used for localization of the ubiquinone binding site [Pohl10]. There may be two ubiquinone binding sites [Verkhovsky12], and NDH-1 purified using a new procedure contained two molecules of ubiquinone per complex [Narayanan13]. A tightly bound ubiquinone found by [Verkhovskaya14] has a very low midpoint potential of < -300 mV, while two quinone radicals found by [Hielscher13] had midpoint potentials of -37 and -235 mV. The NuoJ [Kao05a], NuoK [Kervinen04, Kao05], NuoM [TorresBacete07] and NuoN [Amarneh03] subunits are implicated in the ability to generate an electrochemical gradient. Molecular dynamics simulations of the membrane domain have established a possible coupling mechanism for energy transduction within NDH-1 [Kaila14].

Three-dimensional reconstruction and 2-D crystals of the NDH-1 complex based on cryo-electron microscopy showed an L-shaped form with an integral membrane and a peripheral arm [Guenebaut98, Holt03]. A model of the spatial arrangement of the subunits and the possible functional mechanism of proton pumping has been proposed [Holt03]. Under low ionic strength conditions, the complex appears to adopt a horseshoe-like conformation [Bottcher02]. Cryo-electron microscopy of the membrane domain allowed calculation of a projection structure at 8 Å resolution [Baranova07a]; later, a cryo-EM 3D structure of the intact NDH-1 complex was obtained [Morgan08]. Binding of NADH induces a conformational change in both the membrane and peripheral arm of NDH-1 [Mamedova04, Pohl08]. A mechanism by which the redox reaction of the N2 Fe-S cluster induces a conformational change that may lead to proton translocation has been proposed [Friedrich10].

Heterooligomers of NDH-1 and NDH-2 have been identified by electrophoresis and sucrose gradient centrifugation suggestive of a supramolecular organisation in the membrane [Sousa11].

NDH-1 is required for the anaerobic respiration of NADH using fumarate or DMSO as the terminal electron acceptors, thus implying that the enzyme can transfer electrons to menaquinone [Tran97]. The comparative energy efficiency of utilization of the various components of the aerobic respiratory chain has been examined [Calhoun93, Unden97].

Stolpe and Friedrich [Stolpe04] showed that NDH-1 is primarily an electrogenic proton pump which may have secondary Na+/H+ antiport activity. However, contrary to the generally accepted view, Steuber et al. [Steuber00] suggested that NDH-1 functions primarily as a Na+ pump, a function that can be conveyed by a truncated form of the NuoL subunit alone [Steuber03, Gemperli07].

NDH-1 produces reactive oxygen species, mainly in the form of H2O2, at the NADH dehydrogenase active site, involving the FMN cofactor [Esterhazy08]. NADH-dependent production of hydrogen peroxide is increased in a NuoF E95Q mutant [Knuuti13]. The rate of O2 reduction is dependent on the NAD+/NADH ratio [Esterhazy08].

Purified NDH-1 is activated by detergent and phospholipids [Sinegina05, Stolpe04]. A tightly bound metal, most likely Ca2+, is required for activity [Verkhovskaya11].

Mutants lacking NDH-1 can not compete with wild type in stationary phase [Zambrano93]. Expression of the nuo operon is regulated by oxygen, nitrate, fumarate, and other factors including C4 dicarboxylates [Bongaerts95, Tran97]. Transcription and activity of aerobic respiratory chain components in the different phases of aerobic growth have been measured [Sousa12].

Reviews: [Sato14, NakamaruOgiso14, Sazanov13, Kanjee13, Ohnishi10, Schneider08, Sazanov07, Friedrich04, Yagi03, Friedrich01, Friedrich00, Ohnishi98, Friedrich98, Unden97, Neijssel94, ECOSAL]

Citations: [Wong14, Kriegel14]

Locations: inner membrane

Molecular Weight: 550.0 kD (experimental) [Spehr99]

Relationship Links: PDB:Structure:3M9C

GO Terms:

Biological Process: GO:0009061 - anaerobic respiration Inferred from experiment [Tran97]
GO:0015990 - electron transport coupled proton transport Inferred from experiment [Euro08a]
GO:0019645 - anaerobic electron transport chain Inferred from experiment [Tran97]
GO:0019646 - aerobic electron transport chain Inferred from experiment [FalkKrzesinski98]
GO:0030965 - plasma membrane electron transport, NADH to quinone Inferred from experiment [Pohl07a]
Molecular Function: GO:0005509 - calcium ion binding Inferred from experiment [Verkhovskaya11]
GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred from experiment [Spehr99]
GO:0046583 - cation efflux transmembrane transporter activity Inferred from experiment [Steuber00]
Cellular Component: GO:0045272 - plasma membrane respiratory chain complex I Inferred from experiment [David02]

Last-Curated ? 30-Oct-2014 by Keseler I , SRI International

Enzymatic reaction of: NADH:ubiquinone oxidoreductase (H+-transporting) (NADH:quinone oxidoreductase I)

Synonyms: ubiquinone reductase, NADH dehydrogenase, respiratory-chain NADH dehydrogenase

EC Number:

Transport reaction diagram for NADH:ubiquinone oxidoreductase (H+-transporting)

Alternative Substrates for NADH: nicotinamide hypoxanthine dinucleotide [Matsushita87 ]

Alternative Substrates for a ubiquinone: ubiquinone-8 , ubiquinone-2 [David02 , Braun98 ] , ubiquinone-1 [David02 ]

Alternative Products for an ubiquinol: ubiquinol-8

In Pathways: NADH to cytochrome bd oxidase electron transfer I , NADH to cytochrome bo oxidase electron transfer I

The reaction is reversible in vitro [Poole74], but physiologically unidirectional. The physiological electron acceptor is expected to be ubiquinone-8.

The Km for ubiquinone-2 is 2 µM [Braun98], and for decylubiquinone, 10 µM [Spehr99].

The Ki for piericidin A is 45 nM [Spehr99].

Cofactors or Prosthetic Groups: a [2Fe-2S] iron-sulfur cluster [Braun98, Spehr99, Uhlmann05], a [4Fe-4S] iron-sulfur cluster [Braun98, Spehr99], Ca2+ [Verkhovskaya11], FMN [Hayashi89, Spehr99]

Activators (Unknown Mechanism): K+ [Euro09a]

Inhibitors (Competitive): NAD+ [Euro09]

Inhibitors (Mixed): Zn2+ [Schulte14]

Inhibitors (Unknown Mechanism): La3+ [Euro09a] , piericidin A [David02, Matsushita87, Spehr99] , myxothiazol [Matsushita87] , o-phenanthroline [Finel94] , 3-undecyl-2-hydroxyl-1,4-naphthoquinone [Matsushita87] , capsaicin [Satoh96, Yagi90]

Kinetic Parameters:

Km (μM)

Enzymatic reaction of: NADH:menaquinone oxidoreductase (H+-transporting) (NADH:quinone oxidoreductase I)

EC Number: 1.6.5.-

Transport reaction diagram for NADH:menaquinone oxidoreductase (H+-transporting)

Alternative Substrates for a menaquinone: menaquinone-8

Alternative Products for a menaquinol: menaquinol-8

In Pathways: NADH to trimethylamine N-oxide electron transfer , NADH to dimethyl sulfoxide electron transfer , nitrate reduction VIII (dissimilatory) , NADH to fumarate electron transfer

Sequence Features

Protein sequence of NADH:ubiquinone oxidoreductase, membrane subunit J with features indicated

Feature Class Location Citations Comment
Transmembrane-Region 1 -> 21
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 28 -> 48
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 54 -> 74
UniProt: Helical;; Non-Experimental Qualifier: potential;
Sequence-Conflict 85
[Weidner93, UniProt10]
UniProt: (in Ref. 1; CAA48369);
Transmembrane-Region 92 -> 112
UniProt: Helical;; Non-Experimental Qualifier: potential;
Sequence-Conflict 126
[Weidner93, UniProt10]
UniProt: (in Ref. 1; CAA48369);
Transmembrane-Region 138 -> 158
UniProt: Helical;; Non-Experimental Qualifier: potential;

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b2280 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12090; confirmed by SwissProt match.


Al12: Al Mamun AA, Lombardo MJ, Shee C, Lisewski AM, Gonzalez C, Lin D, Nehring RB, Saint-Ruf C, Gibson JL, Frisch RL, Lichtarge O, Hastings PJ, Rosenberg SM (2012). "Identity and function of a large gene network underlying mutagenic repair of DNA breaks." Science 338(6112);1344-8. PMID: 23224554

Amarneh03: Amarneh B, Vik SB (2003). "Mutagenesis of subunit N of the Escherichia coli complex I. Identification of the initiation codon and the sensitivity of mutants to decylubiquinone." Biochemistry 42(17);4800-8. PMID: 12718520

Archer95: Archer CD, Elliott T (1995). "Transcriptional control of the nuo operon which encodes the energy-conserving NADH dehydrogenase of Salmonella typhimurium." J Bacteriol 1995;177(9);2335-42. PMID: 7730262

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Baranova07a: Baranova EA, Holt PJ, Sazanov LA (2007). "Projection structure of the membrane domain of Escherichia coli respiratory complex I at 8 A resolution." J Mol Biol 366(1);140-54. PMID: 17157874

Belevich14: Belevich N, Belevich G, Verkhovskaya M (2014). "Real-time optical studies of respiratory Complex I turnover." Biochim Biophys Acta 1837(12);1973-1980. PMID: 25283488

Berrisford08: Berrisford JM, Thompson CJ, Sazanov LA (2008). "Chemical and NADH-induced, ROS-dependent, cross-linking between subunits of complex I from Escherichia coli and Thermus thermophilus." Biochemistry 47(39);10262-70. PMID: 18771280

Bogachev96: Bogachev AV, Murtazina RA, Skulachev VP (1996). "H+/e- stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells." J Bacteriol 178(21);6233-7. PMID: 8892824

Bongaerts95: Bongaerts J, Zoske S, Weidner U, Unden G (1995). "Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-N) of Escherichia coli by electron acceptors, electron donors and gene regulators." Mol Microbiol 16(3);521-34. PMID: 7565112

Bottcher02: Bottcher B, Scheide D, Hesterberg M, Nagel-Steger L, Friedrich T (2002). "A novel, enzymatically active conformation of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)." J Biol Chem 277(20);17970-7. PMID: 11880370

Braun98: Braun M, Bungert S, Friedrich T (1998). "Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli." Biochemistry 37(7);1861-7. PMID: 9485311

Calhoun93: Calhoun MW, Oden KL, Gennis RB, de Mattos MJ, Neijssel OM (1993). "Energetic efficiency of Escherichia coli: effects of mutations in components of the aerobic respiratory chain." J Bacteriol 175(10);3020-5. PMID: 8491720

Calhoun93a: Calhoun MW, Gennis RB (1993). "Demonstration of separate genetic loci encoding distinct membrane-bound respiratory NADH dehydrogenases in Escherichia coli." J Bacteriol 1993;175(10);3013-9. PMID: 8387992

Choice95: Choice E, Masin D, Bally MB, Meloche M, Madden TD (1995). "Liposomal cyclosporine. Comparison of drug and lipid carrier pharmacokinetics and biodistribution." Transplantation 1995;60(9);1006-11. PMID: 7491673

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

David02: David P, Baumann M, Wikstrom M, Finel M (2002). "Interaction of purified NDH-1 from Escherichia coli with ubiquinone analogues." Biochim Biophys Acta 1553(3);268-78. PMID: 11997136

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

ECOSAL: "Escherichia coli and Salmonella: Cellular and Molecular Biology." Online edition.

Efremov10: Efremov RG, Baradaran R, Sazanov LA (2010). "The architecture of respiratory complex I." Nature 465(7297);441-5. PMID: 20505720

Efremov11: Efremov RG, Sazanov LA (2011). "Structure of the membrane domain of respiratory complex I." Nature 476(7361);414-20. PMID: 21822288

Erhardt12: Erhardt H, Steimle S, Muders V, Pohl T, Walter J, Friedrich T (2012). "Disruption of individual nuo-genes leads to the formation of partially assembled NADH:ubiquinone oxidoreductase (complex I) in Escherichia coli." Biochim Biophys Acta 1817(6);863-71. PMID: 22063474

Esterhazy08: Esterhazy D, King MS, Yakovlev G, Hirst J (2008). "Production of reactive oxygen species by complex I (NADH:ubiquinone oxidoreductase) from Escherichia coli and comparison to the enzyme from mitochondria." Biochemistry 47(12);3964-71. PMID: 18307315

Euro08: Euro L, Bloch DA, Wikstrom M, Verkhovsky MI, Verkhovskaya M (2008). "Electrostatic interactions between FeS clusters in NADH:ubiquinone oxidoreductase (Complex I) from Escherichia coli." Biochemistry 47(10);3185-93. PMID: 18269245

Euro08a: Euro L, Belevich G, Verkhovsky MI, Wikstrom M, Verkhovskaya M (2008). "Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I)." Biochim Biophys Acta 1777(9):1166-72. PMID: 18590697

Euro09: Euro L, Belevich G, Bloch DA, Verkhovsky MI, Wikstrom M, Verkhovskaya M (2009). "The role of the invariant glutamate 95 in the catalytic site of Complex I from Escherichia coli." Biochim Biophys Acta 1787(1);68-73. PMID: 19061856

Euro09a: Euro L, Belevich G, Wikstrom M, Verkhovskaya M (2009). "High affinity cation-binding sites in Complex I from Escherichia coli." Biochim Biophys Acta 1787(8);1024-8. PMID: 19261245

FalkKrzesinski98: Falk-Krzesinski HJ, Wolfe AJ (1998). "Genetic analysis of the nuo locus, which encodes the proton-translocating NADH dehydrogenase in Escherichia coli." J Bacteriol 180(5);1174-84. PMID: 9495756

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Finel94: Finel M, Majander A (1994). "Studies on the proton-translocating NADH:ubiquinone oxidoreductases of mitochondria and Escherichia coli using the inhibitor 1,10-phenanthroline." FEBS Lett 339(1-2);142-6. PMID: 8313963

Friedrich00: Friedrich T, Scheide D (2000). "The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases." FEBS Lett 479(1-2);1-5. PMID: 10940377

Friedrich01: Friedrich T (2001). "Complex I: a chimaera of a redox and conformation-driven proton pump?." J Bioenerg Biomembr 33(3);169-77. PMID: 11695826

Friedrich04: Friedrich T, Bottcher B (2004). "The gross structure of the respiratory complex I: a Lego System." Biochim Biophys Acta 1608(1);1-9. PMID: 14741580

Friedrich10: Friedrich T, Hellwig P (2010). "Redox-induced conformational changes within the Escherichia coli NADH ubiquinone oxidoreductase (complex I): An analysis by mutagenesis and FT-IR spectroscopy." Biochim Biophys Acta 1797:659-63. PMID: 20214873

Friedrich98: Friedrich T (1998). "The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli." Biochim Biophys Acta 1998;1364(2);134-46. PMID: 9593861

Gemperli07: Gemperli AC, Schaffitzel C, Jakob C, Steuber J (2007). "Transport of Na(+) and K (+) by an antiporter-related subunit from the Escherichia coli NADH dehydrogenase I produced in Saccharomyces cerevisiae." Arch Microbiol 188(5);509-21. PMID: 17583799

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Gong03: Gong X, Xie T, Yu L, Hesterberg M, Scheide D, Friedrich T, Yu CA (2003). "The ubiquinone-binding site in NADH:ubiquinone oxidoreductase from Escherichia coli." J Biol Chem 278(28);25731-7. PMID: 12730198

Guenebaut98: Guenebaut V, Schlitt A, Weiss H, Leonard K, Friedrich T (1998). "Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I)." J Mol Biol 276(1);105-12. PMID: 9514725

Hayashi89: 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(1);62-9. PMID: 2679883

Hellwig00: Hellwig P, Scheide D, Bungert S, Mantele W, Friedrich T (2000). "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 39(35);10884-91. PMID: 10978175

Hielscher13: Hielscher R, Yegres M, Voicescu M, Gnandt E, Friedrich T, Hellwig P (2013). "Characterization of two quinone radicals in the NADH:ubiquinone oxidoreductase from Escherichia coli by a combined fluorescence spectroscopic and electrochemical approach." Biochemistry 52(50);8993-9000. PMID: 24279322

Holt03: Holt PJ, Morgan DJ, Sazanov LA (2003). "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 278(44);43114-20. PMID: 12923180

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kaila14: Kaila VR, Wikstrom M, Hummer G (2014). "Electrostatics, hydration, and proton transfer dynamics in the membrane domain of respiratory complex I." Proc Natl Acad Sci U S A 111(19);6988-93. PMID: 24778264

Kanjee13: Kanjee U, Houry WA (2013). "Mechanisms of acid resistance in Escherichia coli." Annu Rev Microbiol 67;65-81. PMID: 23701194

Kao05: Kao MC, Nakamaru-Ogiso E, Matsuno-Yagi A, Yagi T (2005). "Characterization of the membrane domain subunit NuoK (ND4L) of the NADH-quinone oxidoreductase from Escherichia coli." Biochemistry 44(27);9545-54. PMID: 15996109

Kao05a: Kao MC, Di Bernardo S, Nakamaru-Ogiso E, Miyoshi H, Matsuno-Yagi A, Yagi T (2005). "Characterization of the membrane domain subunit NuoJ (ND6) of the NADH-quinone oxidoreductase from Escherichia coli by chromosomal DNA manipulation." Biochemistry 44(9);3562-71. PMID: 15736965

Kervinen04: Kervinen M, Patsi J, Finel M, Hassinen IE (2004). "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 43(3);773-81. PMID: 14730982

Knuuti13: Knuuti J, Belevich G, Sharma V, Bloch DA, Verkhovskaya M (2013). "A single amino acid residue controls ROS production in the respiratory Complex I from Escherichia coli." Mol Microbiol 90(6);1190-200. PMID: 24325249

Kriegel14: Kriegel S, Uchida T, Osawa M, Friedrich T, Hellwig P (2014). "Biomimetic Environment to Study E. coli Complex I through Surface-Enhanced IR Absorption Spectroscopy." Biochemistry 53(40);6340-7. PMID: 25225967

Leif95: Leif H, Sled VD, Ohnishi T, Weiss H, Friedrich T (1995). "Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli." Eur J Biochem 230(2);538-48. PMID: 7607227

Mamedova04: Mamedova AA, Holt PJ, Carroll J, Sazanov LA (2004). "Substrate-induced conformational change in bacterial complex I." J Biol Chem 279(22);23830-6. PMID: 15037611

Matsushita87: Matsushita K, Ohnishi T, Kaback HR (1987). "NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain." Biochemistry 1987;26(24);7732-7. PMID: 3122832

Medvedev10: Medvedev ES, Couch VA, Stuchebrukhov AA (2010). "Determination of the intrinsic redox potentials of FeS centers of respiratory complex I from experimental titration curves." Biochim Biophys Acta 1797(9):1665-71. PMID: 20513348

Morgan08: Morgan DJ, Sazanov LA (2008). "Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides." Biochim Biophys Acta 1777(7-8);711-8. PMID: 18433710

NakamaruOgiso14: Nakamaru-Ogiso E, Narayanan M, Sakyiama JA (2014). "Roles of semiquinone species in proton pumping mechanism by complex I." J Bioenerg Biomembr 46(4);269-77. PMID: 25077450

Narayanan13: Narayanan M, Gabrieli DJ, Leung SA, Elguindy MM, Glaser CA, Saju N, Sinha SC, Nakamaru-Ogiso E (2013). "Semiquinone and cluster N6 signals in His-tagged proton-translocating NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli." J Biol Chem 288(20);14310-9. PMID: 23543743

Neijssel94: Neijssel OM, Teixeira de Mattos MJ (1994). "The energetics of bacterial growth: a reassessment." Mol Microbiol 13(2);172-82. PMID: 7984099

Ohnishi10: Ohnishi T (2010). "Structural biology: Piston drives a proton pump." Nature 465(7297);428-9. PMID: 20505714

Ohnishi98: Ohnishi T (1998). "Iron-sulfur clusters/semiquinones in complex I." Biochim Biophys Acta 1364(2);186-206. PMID: 9593887

Patsi08: Patsi J, Kervinen M, Finel M, Hassinen IE (2008). "Leber hereditary optic neuropathy mutations in the ND6 subunit of mitochondrial complex I affect ubiquinone reduction kinetics in a bacterial model of the enzyme." Biochem J 409(1);129-37. PMID: 17894548

Pohl07a: Pohl T, Uhlmann M, Kaufenstein M, Friedrich T (2007). "Lambda Red-mediated mutagenesis and efficient large scale affinity purification of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)." Biochemistry 46(37);10694-702. PMID: 17722886

Pohl08: Pohl T, Schneider D, Hielscher R, Stolpe S, Dorner K, Kohlstadt M, Bottcher B, Hellwig P, Friedrich T (2008). "Nucleotide-induced conformational changes in the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)." Biochem Soc Trans 36(Pt 5);971-5. PMID: 18793172

Pohl10: Pohl T, Spatzal T, Aksoyoglu M, Schleicher E, Rostas AM, Lay H, Glessner U, Boudon C, Hellwig P, Weber S, Friedrich T (2010). "Spin labeling of the Escherichia coli NADH ubiquinone oxidoreductase (complex I)." Biochim Biophys Acta. PMID: 20959113

Poole74: Poole RK, Haddock BA (1974). "Energy-linked reduction of nicotinamide--adenine dinucleotide in membranes derived from normal and various respiratory-deficient mutant strains of Escherichia coli K12." Biochem J 144(1);77-85. PMID: 4156832

Sato14: Sato M, Torres-Bacete J, Sinha PK, Matsuno-Yagi A, Yagi T (2014). "Essential regions in the membrane domain of bacterial complex I (NDH-1): the machinery for proton translocation." J Bioenerg Biomembr 46(4);279-87. PMID: 24973951

Satoh96: Satoh T, Miyoshi H, Sakamoto K, Iwamura H (1996). "Comparison of the inhibitory action of synthetic capsaicin analogues with various NADH-ubiquinone oxidoreductases." Biochim Biophys Acta 1273(1);21-30. PMID: 8573592

Sazanov07: Sazanov LA (2007). "Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain." Biochemistry 46(9);2275-88. PMID: 17274631

Sazanov13: Sazanov LA, Baradaran R, Efremov RG, Berrisford JM, Minhas G (2013). "A long road towards the structure of respiratory complex I, a giant molecular proton pump." Biochem Soc Trans 41(5);1265-71. PMID: 24059518

Schneider08: Schneider D, Pohl T, Walter J, Dorner K, Kohlstadt M, Berger A, Spehr V, Friedrich T (2008). "Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)." Biochim Biophys Acta 1777(7-8);735-9. PMID: 18394423

Schulte14: Schulte M, Mattay D, Kriegel S, Hellwig P, Friedrich T (2014). "Inhibition of Escherichia coli Respiratory Complex I by Zn(2+)." Biochemistry 53(40);6332-9. PMID: 25238255

Sinegina05: Sinegina L, Wikstrom M, Verkhovsky MI, Verkhovskaya ML (2005). "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 44(23);8500-6. PMID: 15938640

Sousa11: Sousa PM, Silva ST, Hood BL, Charro N, Carita JN, Vaz F, Penque D, Conrads TP, Melo AM (2011). "Supramolecular organizations in the aerobic respiratory chain of Escherichia coli." Biochimie 93(3);418-25. PMID: 21040753

Sousa12: Sousa PM, Videira MA, Bohn A, Hood BL, Conrads TP, Goulao LF, Melo AM (2012). "The aerobic respiratory chain of Escherichia coli: from genes to supercomplexes." Microbiology 158(Pt 9);2408-18. PMID: 22700653

Spehr99: Spehr V, Schlitt A, Scheide D, Guenebaut V, Friedrich T (1999). "Overexpression of the Escherichia coli nuo-operon and isolation of the overproduced NADH:ubiquinone oxidoreductase (complex I)." Biochemistry 1999;38(49);16261-7. PMID: 10587449

Steimle11: Steimle S, Bajzath C, Dorner K, Schulte M, Bothe V, Friedrich T (2011). "Role of subunit NuoL for proton translocation by respiratory complex I." Biochemistry 50(16);3386-93. PMID: 21417432

Steuber00: Steuber J, Schmid C, Rufibach M, Dimroth P (2000). "Na+ translocation by complex I (NADH:quinone oxidoreductase) of Escherichia coli." Mol Microbiol 2000;35(2);428-34. PMID: 10652103

Steuber03: Steuber J (2003). "The C-terminally truncated NuoL subunit (ND5 homologue) of the Na+-dependent complex I from Escherichia coli transports Na+." J Biol Chem 278(29);26817-22. PMID: 12740360

Stolpe04: Stolpe S, Friedrich T (2004). "The Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is a primary proton pump but may be capable of secondary sodium antiport." J Biol Chem 279(18);18377-83. PMID: 14970214

TorresBacete07: Torres-Bacete J, Nakamaru-Ogiso E, Matsuno-Yagi A, Yagi T (2007). "Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1: Conserved charged residues essential for energy-coupled activities." J Biol Chem 282(51);36914-22. PMID: 17977822

Tran97: Tran QH, Bongaerts J, Vlad D, Unden G (1997). "Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in respiration of NADH to fumarate and its bioenergetic implications." Eur J Biochem 244(1);155-60. PMID: 9063459

Treberg11: Treberg JR, Brand MD (2011). "A model of the proton translocation mechanism of complex I." J Biol Chem 286(20);17579-84. PMID: 21454533

Uhlmann05: Uhlmann M, Friedrich T (2005). "EPR Signals Assigned to Fe/S Cluster N1c of the Escherichia coli NADH:Ubiquinone Oxidoreductase (Complex I) Derive from Cluster N1a." Biochemistry 44(5);1653-8. PMID: 15683249

Unden97: Unden G, Bongaerts J (1997). "Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors." Biochim Biophys Acta 1320(3);217-34. PMID: 9230919

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Verkhovskaya08: Verkhovskaya ML, Belevich N, Euro L, Wikstrom M, Verkhovsky MI (2008). "Real-time electron transfer in respiratory complex I." Proc Natl Acad Sci U S A 105(10);3763-7. PMID: 18316732

Verkhovskaya11: Verkhovskaya M, Knuuti J, Wikstrom M (2011). "Role of Ca(2+) in structure and function of Complex I from Escherichia coli." Biochim Biophys Acta 1807(1);36-41. PMID: 20840839

Verkhovskaya14: Verkhovskaya M, Wikstrom M (2014). "Oxidoreduction properties of bound ubiquinone in Complex I from Escherichia coli." Biochim Biophys Acta 1837(2);246-50. PMID: 24216024

Verkhovsky12: Verkhovsky M, Bloch DA, Verkhovskaya M (2012). "Tightly-bound ubiquinone in the Escherichia coli respiratory complex I." Biochim Biophys Acta 1817(9);1550-6. PMID: 22580197

Weidner93: Weidner U, Geier S, Ptock A, Friedrich T, Leif H, Weiss H (1993). "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(1);109-22. PMID: 7690854

Wikstrom12: Wikstrom M, Hummer G (2012). "Stoichiometry of proton translocation by respiratory complex I and its mechanistic implications." Proc Natl Acad Sci U S A 109(12);4431-6. PMID: 22392981

Wong14: Wong KS, Snider JD, Graham C, Greenblatt JF, Emili A, Babu M, Houry WA (2014). "The MoxR ATPase RavA and Its Cofactor ViaA Interact with the NADH:Ubiquinone Oxidoreductase I in Escherichia coli." PLoS One 9(1);e85529. PMID: 24454883

Yagi03: Yagi T, Matsuno-Yagi A (2003). "The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked." Biochemistry 42(8);2266-74. PMID: 12600193

Yagi90: 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(2);305-11. PMID: 2118334

Zambrano93: Zambrano MM, Kolter R (1993). "Escherichia coli mutants lacking NADH dehydrogenase I have a competitive disadvantage in stationary phase." J Bacteriol 175(17);5642-7. PMID: 8366049

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111

Other References Related to Gene Regulation

Kumar11: Kumar R, Shimizu K (2011). "Transcriptional regulation of main metabolic pathways of cyoA, cydB, fnr, and fur gene knockout Escherichia coli in C-limited and N-limited aerobic continuous cultures." Microb Cell Fact 10;3. PMID: 21272324

Lynch96: Lynch AS, Lin EC (1996). "Transcriptional control mediated by the ArcA two-component response regulator protein of Escherichia coli: characterization of DNA binding at target promoters." J Bacteriol 1996;178(21);6238-49. PMID: 8892825

Marzan13: Marzan LW, Hasan CM, Shimizu K (2013). "Effect of acidic condition on the metabolic regulation of Escherichia coli and its phoB mutant." Arch Microbiol 195(3);161-71. PMID: 23274360

Salmon03: Salmon K, Hung SP, Mekjian K, Baldi P, Hatfield GW, Gunsalus RP (2003). "Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR." J Biol Chem 278(32);29837-55. PMID: 12754220

Salmon05: Salmon KA, Hung SP, Steffen NR, Krupp R, Baldi P, Hatfield GW, Gunsalus RP (2005). "Global gene expression profiling in Escherichia coli K12: effects of oxygen availability and ArcA." J Biol Chem 280(15);15084-96. PMID: 15699038

ShalelLevanon05: Shalel-Levanon S, San KY, Bennett GN (2005). "Effect of oxygen, and ArcA and FNR regulators on the expression of genes related to the electron transfer chain and the TCA cycle in Escherichia coli." Metab Eng 7(5-6):364-74. PMID: 16140031

Wackwitz99: Wackwitz B, Bongaerts J, Goodman SD, Unden G (1999). "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 262(4-5);876-83. PMID: 10628873

Zhang04c: Zhang J, Zeuner Y, Kleefeld A, Unden G, Janshoff A (2004). "Multiple site-specific binding of Fis protein to Escherichia coli nuoA-N promoter DNA and its impact on DNA topology visualised by means of scanning force microscopy." Chembiochem 5(9);1286-9. PMID: 15368583

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Mon Oct 5, 2015, biocyc14.