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Escherichia coli K-12 substr. MG1655 Transporter: 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 [Kao05], NuoK [Kervinen04, Kao05a], 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, Schneider08, 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

Gene-Reaction Schematic: ?

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


Subunit of NADH:ubiquinone oxidoreductase I: NADH:ubiquinone oxidoreductase, membrane subunit A

Synonyms: NuoA

Gene: nuoA Accession Numbers: EG12082 (EcoCyc), b2288, ECK2282

Locations: inner membrane

Sequence Length: 147 AAs

Molecular Weight: 16.457 kD (from nucleotide sequence)

pI: 10.4

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01]
Molecular Function: GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred from experiment Inferred by computational analysis [GOA01, Zambrano93]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016651 - oxidoreductase activity, acting on NAD(P)H Inferred by computational analysis [GOA01]
GO:0048038 - quinone binding Inferred by computational analysis [UniProtGOA11a]
GO:0050136 - NADH dehydrogenase (quinone) activity Inferred by computational analysis [GOA06, GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, DiazMejia09, Zhang07, Leif95]
GO:0005887 - integral component of plasma membrane Inferred from experiment [Virzintiene11]
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]
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

Unification Links: DIP:DIP-59257N , EcoliWiki:b2288 , PR:PRO_000023429 , Pride:P0AFC3 , Protein Model Portal:P0AFC3 , RefSeq:NP_416791 , SMR:P0AFC3 , String:511145.b2288 , UniProt:P0AFC3

Relationship Links: InterPro:IN-FAMILY:IPR000440 , InterPro:IN-FAMILY:IPR023043 , Panther:IN-FAMILY:PTHR11058 , Pfam:IN-FAMILY:PF00507

Summary:
NuoA is part of the inner membrane component of NADH dehydrogenase I [Leif95]. The protein has three predicted transmembrane domains [Kao04], and the C terminus is located in the cytoplasm [Virzintiene11]. Site-specific mutagenesis of conserved charged amino acid residues has elucidated possible functional roles for Asp79 and Glu81 [Kao04]. A crystal structure of the membrane component at higher resolution has allowed better identification of the interactions between the subunits [Efremov11].

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].

NuoA: "NADH:ubiquinone oxidoreductase" [Calhoun93]

Essentiality data for nuoA 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]

Subunit of NADH:ubiquinone oxidoreductase I: NADH:ubiquinone oxidoreductase, membrane subunit H

Synonyms: NuoH

Gene: nuoH Accession Numbers: EG12088 (EcoCyc), b2282, ECK2276

Locations: inner membrane

Sequence Length: 325 AAs

Molecular Weight: 36.219 kD (from nucleotide sequence)

pI: 8.55

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [FalkKrzesinski98]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01]
Molecular Function: GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred by computational analysis
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016655 - oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Inferred by computational analysis [GOA06]
GO:0048038 - quinone binding Inferred by computational analysis [UniProtGOA11a]
GO:0050136 - NADH dehydrogenase (quinone) activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, 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, Spehr99]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01]
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

Unification Links: EcoliWiki:b2282 , PR:PRO_000023435 , Protein Model Portal:P0AFD4 , RefSeq:NP_416785 , SMR:P0AFD4 , String:511145.b2282 , UniProt:P0AFD4

Relationship Links: InterPro:IN-FAMILY:IPR001694 , InterPro:IN-FAMILY:IPR018086 , Panther:IN-FAMILY:PTHR11432 , Pfam:IN-FAMILY:PF00146 , Prosite:IN-FAMILY:PS00667 , Prosite:IN-FAMILY:PS00668

Summary:
NuoH is part of the inner membrane component of NADH dehydrogenase I [Leif95]. The protein has eight predicted transmembrane domains; the C terminus is located in the periplasm [Daley05].

This subunit was thought to contain the ubiquinone binding site [Weidner93, Friedrich98], which has since been proposed to be located in the NuoM subunit [Gong03]. However, an E36Q mutant shows higher apparent Km for ubiquinone, suggesting proximity to the ubiquinone binding domain [Patsi12]. The charged residues of the cytoplasmic loops are highly conserved; mutagenesis of these residues results in loss of enzymatic activity and a low content of the peripheral subunits NuoB and NuoCD, indicating that the cytoplasmic loops are essential for assembly of the peripheral arm of NDH-1 [Sinha09].

The similarity between NDH-1 and the mitochondrial Complex I has been exploited to study the effects of pathogenic mutations and polymorphisms found in the human proteins on enzymatic activity [Maliniemi09, Hinttala10]. An E36K mutation in NuoH (analogous to an E24K mutation in the human mitochondrial protein that is associated with the LHON/MELAS disease phenotype) almost completely abolishes NDH-1 activity [Patsi12].

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

nuoH 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].

NuoH: "NADH:ubiquinone oxidoreductase" [Calhoun93]

Essentiality data for nuoH 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]

Subunit of NADH:ubiquinone oxidoreductase I: NADH:ubiquinone oxidoreductase, membrane subunit J

Synonyms: NuoJ

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

Locations: inner membrane

Sequence Length: 184 AAs

Molecular Weight: 19.875 kD (from nucleotide sequence)

pI: 5.77

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred from experiment Inferred by computational analysis [GOA01, Kao05]
GO:0016491 - oxidoreductase activity 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]
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, Pohl07]
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

Unification Links: DIP:DIP-59258N , EcoliWiki:b2280 , PR:PRO_000023437 , Protein Model Portal:P0AFE0 , RefSeq:NP_416783 , SMR:P0AFE0 , String:511145.b2280 , UniProt:P0AFE0

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

Summary:
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 [Kao05]. 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" [Calhoun93]

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]

Subunit of NADH:ubiquinone oxidoreductase I: NADH:ubiquinone oxidoreductase, membrane subunit K

Synonyms: NuoK

Gene: nuoK Accession Numbers: EG12091 (EcoCyc), b2279, ECK2273

Locations: inner membrane

Sequence Length: 100 AAs

Molecular Weight: 10.845 kD (from nucleotide sequence)

Molecular Weight: 11 kD (experimental) [Kao05a]

pI: 11.9

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0042773 - ATP synthesis coupled electron transport Inferred by computational analysis [GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA06]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Price10]
GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred from experiment [Kao05a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016651 - oxidoreductase activity, acting on NAD(P)H Inferred by computational analysis [GOA01]
GO:0048038 - quinone binding Inferred by computational analysis [UniProtGOA11a]
GO:0050136 - NADH dehydrogenase (quinone) activity Inferred by computational analysis [GOA06, GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, 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, Pohl07]
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

Unification Links: DIP:DIP-51165N , EcoliWiki:b2279 , PR:PRO_000023438 , Protein Model Portal:P0AFE4 , RefSeq:NP_416782 , SMR:P0AFE4 , String:511145.b2279 , UniProt:P0AFE4

Relationship Links: InterPro:IN-FAMILY:IPR001133 , Panther:IN-FAMILY:PTHR11434 , Pfam:IN-FAMILY:PF00420

Summary:
NuoK is part of the inner membrane component of NADH dehydrogenase I [Leif95]. The protein has three 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].

The two membrane-embedded acidic residues Glu36 and Glu72 of NuoK are required for high rates of ubiquinone reduction [Kervinen04]. Glu36 mutants appear to lack electron transfer activity and thus the ability to generate an electrochemical gradient [Kao05a]. Analysis of site-directed mutants in other conserved residues of NuoK has been performed [Kao05a].

The SecYEG protein secretion machinery and its YidC component are required for insertion of NuoK in the cytoplasmic membrane. The YidC requirement is due to the presence of two conserved glutamate residues (E36, E72) in tansmembrane segments of NuoK [Price10].

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

nuoK 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].

NuoK: "NADH:ubiquinone oxidoreductase" [Calhoun93]

Essentiality data for nuoK knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
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]

Subunit of NADH:ubiquinone oxidoreductase I: NADH:ubiquinone oxidoreductase, membrane subunit L

Synonyms: NuoL

Gene: nuoL Accession Numbers: EG12092 (EcoCyc), b2278, ECK2272

Locations: inner membrane

Sequence Length: 613 AAs

Molecular Weight: 66.438 kD (from nucleotide sequence)

pI: 9.11

GO Terms:

Biological Process: GO:0015990 - electron transport coupled proton transport Inferred from experiment [Steimle11]
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:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity 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]
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, Pohl07]
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

Unification Links: DIP:DIP-10388N , EcoliWiki:b2278 , PR:PRO_000023439 , Pride:P33607 , Protein Model Portal:P33607 , RefSeq:NP_416781 , SMR:P33607 , String:511145.b2278 , UniProt:P33607

Relationship Links: InterPro:IN-FAMILY:IPR001516 , InterPro:IN-FAMILY:IPR001750 , InterPro:IN-FAMILY:IPR003945 , InterPro:IN-FAMILY:IPR018393 , Pfam:IN-FAMILY:PF00361 , Pfam:IN-FAMILY:PF00662 , Prints:IN-FAMILY:PR01435

Summary:
NuoL is part of the inner membrane component of NADH dehydrogenase I [Leif95, Baranova07a]. The protein has 14 transmembrane helices and a 110 Å long amphipathic α-helix that spans almost the entire length of the membrane domain [Efremov10]. Transmembrane helices were assigned to locations in the crystal structure using Fourier transform analysis [Vik11]. A crystal structure of the membrane component at higher resolution has allowed better identification of the unusual arrangement of the transmembrane helices [Efremov11].

NuoL was proposed to be located at the distal end of the membrane arm of NDH-1 [Holt03, Baranova07a] and to function in proton translocation [Friedrich98]. Proton translocation may be facilitated by movement of its long amphipathic α-helix, which may result from conformational changes at the interface between the membrane and peripheral domains [Efremov10]. A hypothesis for the involvement of NuoL in proton pumping has been proposed [Ohnishi10a]. However, analysis of an extensive set of NuoL mutants suggests that the amphipathic helix of NuoL does not function as a mechanical piston; it may instead function like a clamp for the NuoLMN subunits during catalytic turnover [Belevich11].

Site-directed mutagenesis of residues that are conserved between NuoL and Na+/H+ antiporters as well as studies using specific inhibitors indicate that NuoL is involved in the indirect coupling mechanism for proton pumping [NakamaruOgiso10]. Site-directed mutagenesis of the three antiporter-like subunits NuoL, M and N indicate that these subunits have a common role in NDH-1 [Michel11, Sato13]. When the NDH-1 complex is reconstituted with NuoL subunits that are truncated at various points in the amphipathic helix, proton translocation is diminished, but not abolished, arguing for at least two coupling sites for proton translocation, with NuoL being essential for the translocation of 2H+/2e- [Steimle11]. However, additional reports using C-terminally truncated forms of NuoL indicated that intact NuoL is required for correct assembly of NDH-1 [TorresBacete11, Belevich11]. Yet, overexpression of all NDH-1 subunits except NuoL is reported to result in formation of a ΔNuoL NDH-1 complex that is capable of the electron transfer reaction, and whose proton translocation activity is approximately half that of wild type [Erhardt12]. A point mutation in the conserved D563 residue within the amphipathic helix of NuoL also results in significantly reduced proton translocation [Steimle12].

The specific functional complementation by NuoL of a B. subtilis ΔmrpA Na+ channel mutant indicates that NuoL may transport Na+ as well [Moparthi11]. A C-terminally truncated fragment of NuoL was previously shown to function as a Na+ pump [Steuber03, Gemperli07].

Null mutants of all individual nuo genes have a growth defect under aerobic conditions in rich medium [Erhardt12]. A nuoL mutant contains two populations of partially assembled complex I, one with electron transfer activity and about half of the proton transfer activity of wild type, and one inactive complex that is associated with CadA [Erhardt12].

nuoL 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].

NuoL: "NADH:ubiquinone oxidoreductase" [Calhoun93]

Review: [Steuber01]

Essentiality data for nuoL 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]

Subunit of NADH:ubiquinone oxidoreductase I: NADH:ubiquinone oxidoreductase, membrane subunit M

Synonyms: NuoA, NuoM

Gene: nuoM Accession Numbers: EG11773 (EcoCyc), b2277, ECK2271

Locations: inner membrane

Sequence Length: 509 AAs

Molecular Weight: 56.525 kD (from nucleotide sequence)

pI: 8.71

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [FalkKrzesinski98]
GO:0015990 - electron transport coupled proton transport Inferred from experiment [Euro08a]
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:0048039 - ubiquinone binding Inferred from experiment [Gong03]
GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity 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]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, 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, Gong03]
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

Unification Links: DIP:DIP-59255N , EcoliWiki:b2277 , PR:PRO_000023440 , Protein Model Portal:P0AFE8 , RefSeq:NP_416780 , SMR:P0AFE8 , String:511145.b2277 , UniProt:P0AFE8

Relationship Links: InterPro:IN-FAMILY:IPR001750 , InterPro:IN-FAMILY:IPR003918 , InterPro:IN-FAMILY:IPR010227 , Pfam:IN-FAMILY:PF00361 , Prints:IN-FAMILY:PR01437

Summary:
NuoM is part of the inner membrane component of NADH dehydrogenase I [Leif95, Baranova07a]. The protein has 14 transmembrane helices [Efremov10]. Transmembrane helices were assigned to locations in the crystal structure using Fourier transform analysis [Vik11]. A crystal structure of the membrane component at higher resolution has allowed better identification of the unusual arrangement of the transmembrane helices [Efremov11].

This subunit may function in proton translocation [Friedrich98] and may contain the ubiquinone binding site [Gong03]. Site-directed mutagenesis of various conserved amino acid residues suggest that E144 and K234 are essential for energy transduction and may thus participate in proton translocation [TorresBacete07, Euro08a]. The E144 residue was systematically shifted to other positions within helix V and adjacent helices by site-directed mutagenesis. When the glutamic acid residue was shifted by one turn of the helix upstream or downstream, a moderate level of energy-transducing activity of NDH-1 was restored [TorresBacete09]. NuoM and NuoN share a pattern of conserved residues; predictions of membrane topology indicate that conserved Lys residues are located in a transmembrane helix and suggest a proton translocation mechanism [Euro08a]. Further site-directed mutagenesis of the three antiporter-like subunits NuoL, M and N indicate that these subunits have a common role in NDH-1 [Michel11, Sato13]. Results with C-terminally truncated forms of NuoM indicated that intact NuoM is required for correct assembly of NDH-1 [TorresBacete11].

The membrane topology of NuoM was investigated using His6 tags; helices X and XI are probably located outside of the membrane, on the cytoplasmic side. The N- and C-terminus of NuoM are located in the periplasm. An overall membrane topology was proposed [TorresBacete09]. NuoM was proposed to be located at the distal end of the membrane arm of NDH-1 [Holt03, Baranova07a].

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

NuoM: "NADH:ubiquinone oxidoreductase" [Calhoun93]

Citations: [Knuuti13]

Essentiality data for nuoM 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]

Subunit of NADH:ubiquinone oxidoreductase I: NADH:ubiquinone oxidoreductase, membrane subunit N

Synonyms: NuoN

Gene: nuoN Accession Numbers: EG12093 (EcoCyc), b2276, ECK2270

Locations: inner membrane

Sequence Length: 485 AAs

Molecular Weight: 52.044 kD (from nucleotide sequence)

pI: 8.47

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [FalkKrzesinski98]
GO:0015990 - electron transport coupled proton transport Inferred from experiment [Sato13]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0042773 - ATP synthesis coupled electron transport Inferred by computational analysis [GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01]
Molecular Function: GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred from experiment Inferred by computational analysis [GOA01, Amarneh03]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0048038 - quinone binding Inferred by computational analysis [UniProtGOA11a]
GO:0050136 - NADH dehydrogenase (quinone) activity Inferred by computational analysis [GOA06, GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, DiazMejia09, 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, David02]
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

Unification Links: DIP:DIP-59256N , EcoliWiki:b2276 , PR:PRO_000023441 , Protein Model Portal:P0AFF0 , RefSeq:NP_416779 , SMR:P0AFF0 , String:511145.b2276 , UniProt:P0AFF0

Relationship Links: InterPro:IN-FAMILY:IPR001750 , InterPro:IN-FAMILY:IPR010096 , Pfam:IN-FAMILY:PF00361

Summary:
NuoN is part of the inner membrane component of NADH dehydrogenase I [Leif95]. The protein has 14 transmembrane helices [Efremov10]. The transmembrane topology of NuoN has been investigated, supporting data from the crystal structure and indicating that both the N and C terminus are located in the periplasm [Amarneh10]. Transmembrane helices were assigned to locations in the crystal structure using Fourier transform analysis [Vik11]. A crystal structure of the membrane component at higher resolution has allowed better identification of the unusual arrangement of the transmembrane helices [Efremov11].

This subunit may function in proton translocation [Friedrich98]. Site-directed mutagenesis has identified residues important for dNADH oxidase activity, proton translocation, and interaction with quinones [Amarneh03]. NuoM and NuoN share a pattern of conserved residues; predictions of membrane topology indicate that conserved Lys residues are located in a transmembrane helix and suggest a proton translocation mechanism [Euro08a]. Further site-directed mutagenesis of the three antiporter-like subunits NuoL, M and N indicate that these subunits have a common role in NDH-1 [Michel11] and likely pump protons by a similar mechanism [Sato13]. The specific functional complementation by NuoN of a B. subtilis ΔmrpD H+ channel mutant indicates that NuoN may transport H+ as well [Moparthi11]. Mutational analysis of the conserved K395 residue suggests that it is involved in H+ transport; the K158 residue is required for interaction with NuoL [Sato13].

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

NuoN: "NADH:ubiquinone oxidoreductase" [Calhoun93]

Citations: [Gustavsson10]

Essentiality data for nuoN 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]

Subunit of NADH:ubiquinone oxidoreductase I: soluble NADH dehydrogenase fragment

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


Subunit of soluble NADH dehydrogenase fragment: NADH:ubiquinone oxidoreductase, chain E

Synonyms: NuoE

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

Locations: inner membrane

Sequence Length: 166 AAs

Molecular Weight: 18.59 kD (from nucleotide sequence)

pI: 5.69

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, GOA01]
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, 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]
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

Unification Links: DIP:DIP-35917N , EcoliWiki:b2285 , ModBase:P0AFD1 , PR:PRO_000023432 , Pride:P0AFD1 , Protein Model Portal:P0AFD1 , RefSeq:NP_416788 , 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

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]

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 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]

Subunit of soluble NADH dehydrogenase fragment: NADH:ubiquinone oxidoreductase, chain F

Synonyms: NuoF

Gene: nuoF Accession Numbers: EG11774 (EcoCyc), b2284, ECK2278

Locations: inner membrane

Sequence Length: 445 AAs

Molecular Weight: 49.292 kD (from nucleotide sequence)

pI: 7.11

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [FalkKrzesinski98]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0051287 - NAD binding Inferred from experiment Inferred by computational analysis [GOA01, Euro09a, Weidner93]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Velazquez05]
GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred by computational analysis [GOA01]
GO:0010181 - FMN binding Inferred by computational analysis [GOA01, Weidner93]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016651 - oxidoreductase activity, acting on NAD(P)H 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]
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

Unification Links: DIP:DIP-10382N , EcoliWiki:b2284 , PR:PRO_000023433 , Pride:P31979 , Protein Model Portal:P31979 , RefSeq:NP_416787 , SMR:P31979 , String:511145.b2284 , UniProt:P31979

Relationship Links: InterPro:IN-FAMILY:IPR001949 , InterPro:IN-FAMILY:IPR011537 , InterPro:IN-FAMILY:IPR011538 , InterPro:IN-FAMILY:IPR019554 , InterPro:IN-FAMILY:IPR019575 , Pfam:IN-FAMILY:PF01512 , Pfam:IN-FAMILY:PF10531 , Pfam:IN-FAMILY:PF10589 , Prosite:IN-FAMILY:PS00644 , Prosite:IN-FAMILY:PS00645 , Smart:IN-FAMILY:SM00928

Summary:
NuoF 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 was predicted to contain the FMN and NADH binding sites [Weidner93, Friedrich98]. Site-directed mutagenesis of the E95 residue in the predicted NADH binding site led to altered binding of NADH and inhibition by NAD+, and a change in the midpoint potential of the FMN cofactor in Complex I [Euro09a]. NADH-dependent production of hydrogen peroxide is increased in the E95Q mutant [Knuuti13]. Evolved E. coli strains that are adapted to higher production of NADPH contain an E138A mutation in NuoF; NDH-1 containing this subunit are able to oxidize both NADH and NADPH [Auriol11]. NuoF was shown to contain the N3 4Fe-4S cluster; the cysteine residues responsible for ligation of the 4Fe-4S cluster were identified by site-directed mutagenesis [Velazquez05].

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

NuoF: "NADH:ubiquinone oxidoreductase" [Calhoun93]

Essentiality data for nuoF 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]

Subunit of soluble NADH dehydrogenase fragment: NADH:ubiquinone oxidoreductase, chain G

Synonyms: NuoG

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

Locations: inner membrane

Sequence Length: 908 AAs

Molecular Weight: 100.3 kD (from nucleotide sequence)

pI: 8.8

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, Pohl07a, 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

Unification Links: DIP:DIP-10383N , EcoliWiki:b2283 , Mint:MINT-1244767 , ModBase:P33602 , PR:PRO_000023434 , Pride:P33602 , Protein Model Portal:P33602 , RefSeq:NP_416786 , 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

Summary:
NuoG is part of the soluble fragment of NADH dehydrogenase I, which represents the electron input part of the enzyme [Leif95, Braun98]. 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 [Pohl07a]. The cysteine residues responsible for ligation of the 4Fe-4S clusters were identified by site-directed mutagenesis [NakamaruOgiso05, Pohl07a]. 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]

Essentiality data for nuoG 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]

Subunit of NADH:ubiquinone oxidoreductase I: connecting fragment of NADH dehydrogenase I

Summary:
This complex is thought to connect the soluble fragment of NADH dehydrogenase I to the inner membrane components [Leif95].


Subunit of connecting fragment of NADH dehydrogenase I: NADH:ubiquinone oxidoreductase, chain B

Synonyms: NuoB

Gene: nuoB Accession Numbers: EG12083 (EcoCyc), b2287, ECK2281

Locations: inner membrane

Sequence Length: 220 AAs

Molecular Weight: 25.056 kD (from nucleotide sequence)

pI: 5.83

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [FalkKrzesinski98]
GO:0015990 - electron transport coupled proton transport Inferred from experiment [Flemming06]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01]
Molecular Function: GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred from experiment Inferred by computational analysis [GOA01, FalkKrzesinski98]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Flemming03a]
GO:0005506 - iron ion binding Inferred by computational analysis [GOA06]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0048038 - quinone binding Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0050136 - NADH dehydrogenase (quinone) activity Inferred by computational analysis [GOA06, 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, GOA06, Leif95]
GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Lasserre06]
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

Unification Links: EcoliWiki:b2287 , ModBase:P0AFC7 , PR:PRO_000023430 , Pride:P0AFC7 , Protein Model Portal:P0AFC7 , RefSeq:NP_416790 , SMR:P0AFC7 , String:511145.b2287 , Swiss-Model:P0AFC7 , UniProt:P0AFC7

Relationship Links: InterPro:IN-FAMILY:IPR006137 , InterPro:IN-FAMILY:IPR006138 , InterPro:IN-FAMILY:IPR014406 , Panther:IN-FAMILY:PTHR11995 , Pfam:IN-FAMILY:PF01058 , Prosite:IN-FAMILY:PS01150

Summary:
NuoB is part of the connecting fragment of NADH dehydrogenase I [Leif95].

This subunit contains the N2 4Fe-4S cluster [Weidner93, Friedrich98, Flemming03a], which may play a role in proton translocation activity of NDH I [Hellwig00]. The Glu67 residue is most likely protonated by oxidation of the N2 cluster, and is involved in proton translocation [Flemming06]. A mechanism by which the redox reaction at the N2 cluster induces conformational changes leading to proton translocation has been proposed [Friedrich10].

Point mutations in NuoB have been analyzed; the Tyr114 and Tyr139 residues appear to be protonated upon reduction of the 4Fe-4S cluster, and a double mutant retains only 20% activity [Flemming03]. Mutagenesis of the conserved acidic residues E67, D77, and D94 abolishes electron transfer activity of NDH I [Flemming06]. Enzymes containing these mutant subunits have been characterized by FT-IR difference spectroscopy to evaluate conformational changes [Friedrich10].

In the presence of NADH or reducing agents, crosslinking between NuoB and NuoI in the intact Complex I is abolished, indicating a conformational change involving the hydrophilic subunits in the presence of NADH [Berrisford08].

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

NuoB: "NADH:ubiquinone oxidoreductase" [Calhoun93]

Review: [Flemming05]

Essentiality data for nuoB 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]

Subunit of connecting fragment of NADH dehydrogenase I: NADH:ubiquinone oxidoreductase, chain CD

Synonyms: NuoD, NuoCD, NuoC

Gene: nuoC Accession Numbers: EG12084 (EcoCyc), b2286, ECK2280

Locations: inner membrane

Sequence Length: 596 AAs

Molecular Weight: 68.236 kD (from nucleotide sequence)

Molecular Weight: 65.0 kD (experimental) [Braun98]

pI: 8.49

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Stenberg05, Zarbiv12]
GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred from experiment Inferred by computational analysis [GOA01, CastroGuerrero10]
GO:0003824 - catalytic activity Inferred by computational analysis [UniProtGOA11a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016651 - oxidoreductase activity, acting on NAD(P)H Inferred by computational analysis [GOA01]
GO:0048038 - quinone binding Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0050136 - NADH dehydrogenase (quinone) activity Inferred by computational analysis [GOA06, GOA01a, GOA01]
GO:0051287 - NAD binding Inferred by computational analysis [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, Leif95]
GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Lasserre06]
GO:0030964 - NADH dehydrogenase complex Inferred from experiment Inferred by computational analysis [GOA01, 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

Unification Links: DIP:DIP-10380N , EcoliWiki:b2286 , Mint:MINT-1269278 , ModBase:P33599 , PR:PRO_000023431 , Pride:P33599 , Protein Model Portal:P33599 , RefSeq:NP_416789 , SMR:P33599 , String:511145.b2286 , Swiss-Model:P33599 , UniProt:P33599

Relationship Links: InterPro:IN-FAMILY:IPR001135 , InterPro:IN-FAMILY:IPR001268 , InterPro:IN-FAMILY:IPR010218 , InterPro:IN-FAMILY:IPR014029 , InterPro:IN-FAMILY:IPR020396 , InterPro:IN-FAMILY:IPR022885 , InterPro:IN-FAMILY:IPR023062 , Pfam:IN-FAMILY:PF00329 , Pfam:IN-FAMILY:PF00346 , ProDom:IN-FAMILY:PD001581 , Prosite:IN-FAMILY:PS00535 , Prosite:IN-FAMILY:PS00542

Summary:
NuoC is part of the connecting fragment of NADH dehydrogenase I [Leif95].

Unlike in other bacteria, which contain two separate genes encoding the NuoC and NuoD subunits, the nuoC gene of E. coli K-12 encodes a fused version of these subunits [Braun98]. NuoC is the only subunit of the peripheral arm that does not contain a cofactor. This subunit was predicted to function as the proton channel [Friedrich98]. NuoC interacts with FliG and FliM, components of the flagellar switch-motor complex [Zarbiv12].

Mutagenesis of two conserved histidine residues, H224 and H228, only has a modest effect on ubiquinone reductase activity of NDH-1. An R274A mutant leads to a significant loss of signal from the N2 4Fe-4S cluster as well as from a second fast-relaxing 4Fe-4S cluster [Belevich07a]. Mutagenesis of several highly conserved amino acid residues in the NuoC domain showed that certain Glu and Asp residues are required for energy transduction of NDH-1, as well as for assembly of the enzyme [CastroGuerrero10].

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

nuoC 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].

NuoC: "NADH:ubiquinone oxidoreductase" [Calhoun93]

Citations: [Knuuti13]

Essentiality data for nuoC 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]

Subunit of connecting fragment of NADH dehydrogenase I: NADH:ubiquinone oxidoreductase, chain I

Synonyms: NuoI

Gene: nuoI Accession Numbers: EG12089 (EcoCyc), b2281, ECK2275

Locations: inner membrane

Sequence Length: 180 AAs

Molecular Weight: 20.538 kD (from nucleotide sequence)

pI: 7.82

GO Terms:

Biological Process: GO:0009060 - aerobic respiration Inferred from experiment [FalkKrzesinski98]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01]
Molecular Function: GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Sinha12a, Weidner93]
GO:0005506 - iron ion binding Inferred by computational analysis [GOA06]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016651 - oxidoreductase activity, acting on NAD(P)H 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 [GOA06, 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, GOA06, Zhang07, 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

Unification Links: DIP:DIP-35918N , EcoliWiki:b2281 , ModBase:P0AFD6 , PR:PRO_000023436 , Pride:P0AFD6 , Protein Model Portal:P0AFD6 , RefSeq:NP_416784 , SMR:P0AFD6 , String:511145.b2281 , Swiss-Model:P0AFD6 , UniProt:P0AFD6

Relationship Links: InterPro:IN-FAMILY:IPR001450 , InterPro:IN-FAMILY:IPR010226 , InterPro:IN-FAMILY:IPR017896 , InterPro:IN-FAMILY:IPR017900 , Pfam:IN-FAMILY:PF00037 , Prosite:IN-FAMILY:PS00198 , Prosite:IN-FAMILY:PS51379

Summary:
NuoI is part of the connecting fragment of NADH dehydrogenase I [Leif95] and is required for efficient assembly of NDH-1 [Sinha12a]. The Fe-S clusters of NuoI conduct electrons from NuoG to the Fe-S cluster of NuoB [Sinha12a].

Based on sequence similarity, this subunit was predicted to contain the two 4Fe-4S clusters N6a and N6b [Weidner93, Friedrich98, Rasmussen01]. EPR signals for both N6a and N6b have now been detected [Sousa12]. Although N6a and N6b are located close to each other, they display no spin-spin interaction [Sinha12a]. The location and identity of EPR spectra for the N4 and N5 Fe-S clusters were subject of some controversy. The 4Fe-4S cluster N4, located on the NuoG subunit, was thought to be identical to either N6a or N6b [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].

In the presence of NADH or reducing agents, crosslinking between NuoB and NuoI in the intact Complex I is abolished, indicating a conformational change involving the hydrophilic subunits in the presence of NADH [Berrisford08].

Point mutants in the cysteine residues predicted to coordinate the Fe-S clusters and in highly conserved acidic residues have been studied [Sinha12a]. Null mutants of all individual nuo genes have a growth defect under aerobic conditions in rich medium [Erhardt12].

NuoI: "NADH:ubiquinone oxidoreductase" [Calhoun93]

Citations: [Allison11]

Essentiality data for nuoI knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]

References

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