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MetaCyc Polypeptide: NADH:ubiquinone oxidoreductase, chain G

Gene: nuoG Accession Numbers: EG12087 (MetaCyc), b2283, ECK2277

Species: Escherichia coli K-12 substr. MG1655

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

Summary:
NuoG is part of the soluble fragment of NADH dehydrogenase I, which represents the electron input part of the enzyme [Leif95, Braun98a]. NuoG is essential for NDH-1 function [FalkKrzesinski98].

This subunit contains the 2Fe-2S cluster N1b [Yakovlev07] and three 4Fe-4S clusters. N7 was formerly misidentified as "N1c", whose EPR signal is in fact derived from the 2Fe-2S cluster N1a on the NuoE subunit [Uhlmann05, Yakovlev07]. N7 is non-conserved and not thought to be involved in electron transfer; however, it is essential for the stability of NDH-1 [Pohl07]. The cysteine residues responsible for ligation of the 4Fe-4S clusters were identified by site-directed mutagenesis [NakamaruOgiso05, Pohl07]. However, the location and identity of EPR spectra for the N4 and N5 Fe-S clusters were subject of some controversy [Yakovlev07]. Recent reevaluation of the data [Ohnishi08] and mutational analysis of the N5 His(Cys)3 ligands confirmed the location of both N4 and N5 in the NuoG subunit [NakamaruOgiso08].

NuoG is involved in the increased organic solvent tolerance (OTS) mechanism in the crp and cyaA mutants [Okochi08].

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

nuoG 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].

NuoG: "NADH:ubiquinone oxidoreductase" [Calhoun93]

Locations: inner membrane

Map Position: [2,395,461 <- 2,398,187]

Molecular Weight of Polypeptide: 100.3 kD (from nucleotide sequence)

pI: 8.8

Unification Links: ASAP:ABE-0007543 , CGSC:32661 , DIP:DIP-10383N , EchoBASE:EB2011 , EcoGene:EG12087 , EcoliWiki:b2283 , Mint:MINT-1244767 , ModBase:P33602 , OU-Microarray:b2283 , PortEco:nuoG , PR:PRO_000023434 , Pride:P33602 , Protein Model Portal:P33602 , RefSeq:NP_416786 , RegulonDB:EG12087 , SMR:P33602 , String:511145.b2283 , UniProt:P33602

Relationship Links: InterPro:IN-FAMILY:IPR000283 , InterPro:IN-FAMILY:IPR001041 , InterPro:IN-FAMILY:IPR006656 , InterPro:IN-FAMILY:IPR006657 , InterPro:IN-FAMILY:IPR006963 , InterPro:IN-FAMILY:IPR009010 , InterPro:IN-FAMILY:IPR010228 , InterPro:IN-FAMILY:IPR012675 , InterPro:IN-FAMILY:IPR019574 , Pfam:IN-FAMILY:PF00384 , Pfam:IN-FAMILY:PF01568 , Pfam:IN-FAMILY:PF04879 , Pfam:IN-FAMILY:PF10588 , Prosite:IN-FAMILY:PS00197 , Prosite:IN-FAMILY:PS00641 , Prosite:IN-FAMILY:PS00642 , Prosite:IN-FAMILY:PS00643 , Prosite:IN-FAMILY:PS51085 , Prosite:IN-FAMILY:PS51669 , Smart:IN-FAMILY:SM00926 , Smart:IN-FAMILY:SM00929

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [FalkKrzesinski98]
GO:0042773 - ATP synthesis coupled electron transport Inferred by computational analysis [GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06, Stenberg05]
GO:0051537 - 2 iron, 2 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Yakovlev07]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Yakovlev07, Pohl07, NakamaruOgiso05, NakamaruOgiso08]
GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred by computational analysis [GOA01, Gaudet10]
GO:0009055 - electron carrier activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016651 - oxidoreductase activity, acting on NAD(P)H Inferred by computational analysis [GOA01]
GO:0030151 - molybdenum ion binding Inferred by computational analysis [GOA01]
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 [GOA01a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Leif95]
GO:0030964 - NADH dehydrogenase complex Inferred from experiment [Leif95]
GO:0045272 - plasma membrane respiratory chain complex I Inferred from experiment [Erhardt12, David02]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01]

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

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Subunit of: soluble NADH dehydrogenase fragment

Species: Escherichia coli K-12 substr. MG1655

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, Braun98a, Bungert99].

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Subunit of: NADH:ubiquinone oxidoreductase I

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

Species: Escherichia coli K-12 substr. MG1655

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 [Braun98a]; 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 [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, 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 [Friedrich].

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, Schneider08, Sazanov07, Friedrich04, Yagi03, Friedrich01, Friedrich00a, 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 [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]

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , 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 , Braun98a ] , 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

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

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 [Braun98a], and for decylubiquinone, 10 µM [Spehr99].

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

Cofactors or Prosthetic Groups: Ca2+ [Verkhovskaya11], FMN [Hayashi89, Spehr99], [2Fe-2S] iron-sulfur cluster [Braun98a, Spehr99, Uhlmann05], a [4Fe-4S] iron-sulfur cluster [Braun98a, Spehr99]

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

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Link97]
 
Conserved-Region 2 -> 83
[UniProt09]
UniProt: 2Fe-2S ferredoxin-type;
Chain 2 -> 908
[UniProt09]
UniProt: NADH-quinone oxidoreductase subunit G;
Metal-Binding-Site 34
[UniProt10]
UniProt: Iron-sulfur 1 (2Fe-2S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 45
[UniProt10]
UniProt: Iron-sulfur 1 (2Fe-2S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 48
[UniProt10]
UniProt: Iron-sulfur 1 (2Fe-2S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 67
[UniProt10]
UniProt: Iron-sulfur 1 (2Fe-2S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 99
[UniProt10]
UniProt: Iron-sulfur 2 (4Fe-4S); via pros nitrogen; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 103
[UniProt10]
UniProt: Iron-sulfur 2 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 106
[UniProt10]
UniProt: Iron-sulfur 2 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 112
[UniProt10]
UniProt: Iron-sulfur 2 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 151
[UniProt10]
UniProt: Iron-sulfur 3 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 154
[UniProt10]
UniProt: Iron-sulfur 3 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 157
[UniProt10]
UniProt: Iron-sulfur 3 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Sequence-Conflict 188
[Weidner93, UniProt10a]
Alternate sequence: Q; UniProt: (in Ref. 1; CAA48366);
Metal-Binding-Site 201
[UniProt10]
UniProt: Iron-sulfur 3 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Sequence-Conflict 210
[Weidner93, UniProt10a]
Alternate sequence: K; UniProt: (in Ref. 1; CAA48366);
Conserved-Region 221 -> 277
[UniProt13]
UniProt: 4Fe-4S Mo/W bis-MGD-type.
Metal-Binding-Site 228
[UniProt10]
UniProt: Iron-sulfur 4 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 231
[UniProt10]
UniProt: Iron-sulfur 4 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 235
[UniProt10]
UniProt: Iron-sulfur 4 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 263
[UniProt10]
UniProt: Iron-sulfur 4 (4Fe-4S); Non-Experimental Qualifier: by similarity;
Sequence-Conflict 390
[Weidner93, UniProt10a]
Alternate sequence: missing; UniProt: (in Ref. 1; CAA48366);
Sequence-Conflict 648
[Weidner93, UniProt10a]
Alternate sequence: T; UniProt: (in Ref. 1; CAA48366);

History:
Ingrid Keseler on Fri Jun 8, 2007:
Corrected start site based on [Leif95 , Link97 ].
10/20/97 Gene b2283 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12087; confirmed by SwissProt match.


References

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

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

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

Braun98a: 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

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: 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

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