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Escherichia coli K-12 substr. MG1655 Polypeptide: NADH:ubiquinone oxidoreductase, chain E



Gene: nuoE Accession Numbers: EG12086 (EcoCyc), b2285, ECK2279

Regulation Summary Diagram: ?

Component of:
soluble NADH dehydrogenase fragment (summary available)
NADH:ubiquinone oxidoreductase I (extended summary available)

Summary:
NuoE is part of the soluble fragment of NADH dehydrogenase I, which represents the electron input part of the enzyme [Leif95, Braun98].

Based on sequence similarity, this subunit is predicted to contain the N1a 2Fe-2S cluster [Weidner93, Friedrich98, Uhlmann05, Velazquez05].

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

NuoE: "NADH:ubiquinone oxidoreductase" [Calhoun93]

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

Locations: inner membrane

Map Position: [2,399,574 <- 2,400,074] (51.72 centisomes)
Length: 501 bp / 166 aa

Molecular Weight of Polypeptide: 18.59 kD (from nucleotide sequence)

pI: 5.69

Unification Links: ASAP:ABE-0007547 , CGSC:32667 , DIP:DIP-35917N , EchoBASE:EB2010 , EcoGene:EG12086 , EcoliWiki:b2285 , ModBase:P0AFD1 , OU-Microarray:b2285 , PortEco:nuoE , PR:PRO_000023432 , Pride:P0AFD1 , Protein Model Portal:P0AFD1 , RefSeq:NP_416788 , RegulonDB:EG12086 , SMR:P0AFD1 , String:511145.b2285 , UniProt:P0AFD1

Relationship Links: InterPro:IN-FAMILY:IPR002023 , InterPro:IN-FAMILY:IPR012336 , Panther:IN-FAMILY:PTHR10371 , Pfam:IN-FAMILY:PF01257 , Prosite:IN-FAMILY:PS01099

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0022904 - respiratory electron transport chain Inferred by computational analysis [Gaudet10]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06]
GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred by computational analysis [Gaudet10]
GO:0009055 - electron carrier activity Inferred by computational analysis [Gaudet10]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0048038 - quinone binding Inferred by computational analysis [UniProtGOA11a]
GO:0050136 - NADH dehydrogenase (quinone) activity Inferred by computational analysis [GOA01]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a]
GO:0051537 - 2 iron, 2 sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, Friedrich98]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment [Leif95]
GO:0030964 - NADH dehydrogenase complex Inferred from experiment [Leif95]
GO:0045272 - plasma membrane respiratory chain complex I Inferred from experiment [Erhardt12, David02]

MultiFun Terms: 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 nuoE knockouts: ?

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

Credits:
Last-Curated ? 30-Nov-2011 by Keseler I , SRI International


Subunit of: soluble NADH dehydrogenase fragment

Subunit composition of soluble NADH dehydrogenase fragment = [NuoE][NuoF][NuoG]
         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)

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

Summary:
The soluble NADH dehydrogenase fragment represents the electron input part of NADH dehydrogenase I [Leif95, Braun98, Bungert99].


Subunit of: NADH:ubiquinone oxidoreductase I

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

Subunit composition of NADH:ubiquinone 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)

Summary:
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, Calhoun93]

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].

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 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 [Baranova07]. 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 [Verkhovskaya13] 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, Kao05b], NuoM [TorresBacete07] and NuoN [Amarneh03] subunits are implicated in the ability to generate an electrochemical gradient.

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 [Baranova07]; 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 [Calhoun93a, 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. 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, Sazanov13, Kanjee13, Ohnishi10, Schneider08a, Sazanov07, Friedrich04, Yagi03, Friedrich01, Friedrich00, Ohnishi98, Friedrich98, Unden97, Neijssel94, ECOSAL]

Citations: [Knuuti13]

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 [Pohl07]
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]

Credits:
Last-Curated ? 04-Dec-2013 by Keseler I , SRI International


Enzymatic reaction of: NADH:ubiquinone oxidoreductase

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

EC Number: 1.6.5.3

Alternative Substrates for NADH: d-NADH [Matsushita87 ]

Alternative Substrates for an 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

Summary:
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 [4Fe-4S] iron-sulfur cluster [Braun98, Spehr99], Ca2+ [Verkhovskaya11], FMN [Hayashi89, Spehr99], [2Fe-2S] iron-sulfur cluster [Braun98, Spehr99, Uhlmann05]

Activators (Unknown Mechanism): K+ [Euro09]

Inhibitors (Competitive): NAD+ [Euro09a]

Inhibitors (Unknown Mechanism): La3+ [Euro09] , piericidin A [David02, Matsushita87, Spehr99] , myxothiazol [Matsushita87] , o-phenanthroline [Finel94] , 3-undecyl-2-hydroxyl-1,4-naphthoquinone [Matsushita87] , capsaicin [Satoh96, Yagi90]

Kinetic Parameters:

Substrate
Km (μM)
Citations
NADH
5.0
[Spehr99]


Enzymatic reaction of: NADH:menaquinone oxidoreductase (NADH:ubiquinone oxidoreductase I)

EC Number: 1.6.5.-

Alternative Substrates for a menaquinone: menaquinone-8

Alternative Products for a menaquinol: menaquinol-8

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


Sequence Features

Feature Class Location Citations Comment
Sequence-Conflict 22
[Weidner93, UniProt10]
Alternate sequence: I → V; UniProt: (in Ref. 1; CAA48364);
Metal-Binding-Site 92
[UniProt10a]
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: potential;
Metal-Binding-Site 97
[UniProt10a]
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: potential;
Metal-Binding-Site 133
[UniProt10a]
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: potential;
Metal-Binding-Site 137
[UniProt10a]
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: potential;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b2285 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12086; confirmed by SwissProt match.


References

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

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

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

Baranova07: 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

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

Bungert99: Bungert S, Krafft B, Schlesinger R, Friedrich T (1999). "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(2);207-11. PMID: 10544236

Calhoun93: 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

Calhoun93a: 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

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

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

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, 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

Euro09a: 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

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

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

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

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

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. 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

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

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

Kao05b: 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

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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

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Other References Related to Gene Regulation

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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