Record Information
Version 1.0
Update Date 1/22/2018 12:54:54 PM
Metabolite IDPAMDB001653
Identification
Name: Menaquinol 8
Description:Menaquinol 8 is a polyprenylhydroquinone having a an octaprenyl moiety at position 2 and a methyl group at position 3. It is a substrate for Dimethyl sulfoxide reductase (dmsA). This enzyme catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS) using the following reaction: Dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol. DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. This enzyme allows P. aeruginosa to grow anaerobically on DMSO as respiratory oxidant. Menaquinol 8 is generated by Ubiquinone/menaquinone biosynthesis methyltransferase (ubiE). This enzyme is required for the conversion of demethylmenaquinone (DMKH2) to menaquinone (MKH2) and has the following catalytic activity: A demethylmenaquinone + S-adenosyl-L-methionine = a menaquinol + S-adenosyl-L-homocysteine.
Structure
Thumb
Synonyms:
  • MKH2-8
  • Reduced menaquinone-8
Chemical Formula: C51H74O2
Average Molecular Weight: 719.1321
Monoisotopic Molecular Weight: 718.568881612
InChI Key: OIEZRVBFVPGODT-WQWYCSGDSA-N
InChI:InChI=1S/C51H74O2/c1-38(2)20-13-21-39(3)22-14-23-40(4)24-15-25-41(5)26-16-27-42(6)28-17-29-43(7)30-18-31-44(8)32-19-33-45(9)36-37-47-46(10)50(52)48-34-11-12-35-49(48)51(47)53/h11-12,20,22,24,26,28,30,32,34-36,52-53H,13-19,21,23,25,27,29,31,33,37H2,1-10H3/b39-22+,40-24+,41-26+,42-28+,43-30+,44-32+,45-36+
CAS number: Not Available
IUPAC Name:2-methyl-3-[(2E,6E,10E,14E,18E,22E,26E)-3,7,11,15,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaen-1-yl]naphthalene-1,4-diol
Traditional IUPAC Name: menaquinol-8
SMILES:[H]\C(CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC\C(C)=C(/[H])CC1=C(O)C2=CC=CC=C2C(O)=C1C)=C(\C)CCC=C(C)C
Chemical Taxonomy
Taxonomy DescriptionThis compound belongs to the class of organic compounds known as polyprenyl quinols. These are compounds containing a polyisoprene chain attached to a quinol(hydroquinone) at the second ring position.
Kingdom Organic compounds
Super ClassLipids and lipid-like molecules
Class Prenol lipids
Sub ClassQuinone and hydroquinone lipids
Direct Parent Polyprenyl quinols
Alternative Parents
Substituents
  • Polyprenylbenzoquinol
  • Polyprenylphenol
  • 1-naphthol
  • Naphthalene
  • Hydroquinone
  • Benzenoid
  • Hydrocarbon derivative
  • Organooxygen compound
  • Aromatic homopolycyclic compound
Molecular Framework Aromatic homopolycyclic compounds
External Descriptors
Physical Properties
State: Not Available
Charge:0
Melting point: Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility0.000233 mg/mLALOGPS
logP9.92ALOGPS
logP16.22ChemAxon
logS-6.5ALOGPS
pKa (Strongest Acidic)9.38ChemAxon
pKa (Strongest Basic)-6ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count2ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area40.46 Å2ChemAxon
Rotatable Bond Count23ChemAxon
Refractivity242.37 m3·mol-1ChemAxon
Polarizability93.44 Å3ChemAxon
Number of Rings2ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations: Membrane
Reactions:
Hydrogen ion + Menaquinol 8 + Trimethylamine N-Oxide > Water + Menaquinone 8 + Trimethylamine
2 Hydrogen ion + Hydrogen (gas) + Menaquinone 8 > Menaquinol 8 +2 Hydrogen ion
2 Hydrogen ion + Menaquinol 8 + Nitrate > Water + Menaquinone 8 + Nitrite +2 Hydrogen ion
2 Hydrogen ion + Menaquinone 8 + Formic acid > Menaquinol 8 + Carbon dioxide + Hydrogen ion
Dimethyl sulfoxide + Menaquinol 8 > Dimethyl sulfide + Water + Menaquinone 8
Menaquinol 8 + Nitrate > Menaquinone 8 + Water + Nitrite
2 Hydrogen ion + Menaquinol 8 + Oxygen > Water + Menaquinone 8 +2 Hydrogen ion
Menaquinol 8 + Selenocystathionine > Water + Menaquinone 8 + Selenite
Glycerol 3-phosphate + Menaquinone 8 > Dihydroxyacetone phosphate + Menaquinol 8
4 Hydrogen ion + Menaquinone 8 + NADH > Menaquinol 8 + NAD +3 Hydrogen ion
Glycolic acid + Menaquinone 8 > Glyoxylic acid + Menaquinol 8
L-Lactic acid + Menaquinone 8 > Menaquinol 8 + Pyruvic acid
Menaquinone 8 + periplasmic protein disulfide isomerase I (reduced) > Menaquinol 8 + periplasmic protein disulfide isomerase I (oxidized)
3 Menaquinol 8 + 2 Hydrogen ion + Nitrite >3 Menaquinone 8 +2 Water + Ammonium
Fumaric acid + Menaquinol 8 > Menaquinone 8 + Succinic acid
4,5-Dihydroorotic acid + Menaquinone 8 > Menaquinol 8 + Orotic acid
Hydrogen ion + Menaquinone 8 + NADH > Menaquinol 8 + NAD
L-Malic acid + Menaquinone 8 > Menaquinol 8 + Oxalacetic acid
L-Aspartic acid + Menaquinone 8 > Hydrogen ion + Iminoaspartic acid + Menaquinol 8
Hydrogen ion + Menaquinone 8 + NADPH > Menaquinol 8 + NADP
Menaquinol 8 + 2 Oxygen >2 Hydrogen ion + Menaquinone 8 +2 Superoxide anion
2-Demethylmenaquinol 8 + S-Adenosylmethionine > S-Adenosylhomocysteine + Hydrogen ion + Menaquinol 8

Pathways: Not Available
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-014i-0322233900-078712e5ae1a120e9bb4View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-003f-0659682000-b17f6a9f6282acdc780aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-00ls-1579781000-2f32691d12e0c6589b72View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-014i-0000000900-7cce8314869d82157486View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-014i-0100001900-d530f7b545c4e49db453View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0uk9-0912141700-dbc44459a9094ccd680fView in MoNA
References
References:
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
Synthesis Reference: Not Available
Material Safety Data Sheet (MSDS) Not Available
External Links:
ResourceLink
CHEBI ID61684
HMDB IDNot Available
Pubchem Compound ID45479636
Kegg IDNot Available
ChemSpider ID26332321
Wikipedia IDNot Available
BioCyc IDREDUCED-MENAQUINONE
EcoCyc IDREDUCED-MENAQUINONE

Enzymes

General function:
Involved in oxidation-reduction process
Specific function:
Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Does not couple the redox reaction to proton translocation
Gene Name:
ndh
Locus Tag:
PA4538
Molecular weight:
47.4 kDa
Reactions
NADH + acceptor = NAD(+) + reduced acceptor.
General function:
Involved in oxidoreductase activity
Specific function:
The nitrate reductase enzyme complex allows Pseudomonas aeruginosa to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction
Gene Name:
narG
Locus Tag:
PA3875
Molecular weight:
141 kDa
Reactions
Nitrite + acceptor = nitrate + reduced acceptor.
General function:
Involved in catalytic activity
Specific function:
(S)-dihydroorotate + a quinone = orotate + a quinol
Gene Name:
pyrD
Locus Tag:
PA3050
Molecular weight:
36.1 kDa
Reactions
(S)-dihydroorotate + a quinone = orotate + a quinol.
General function:
Involved in electron carrier activity
Specific function:
Formate dehydrogenase allows Pseudomonas aeruginosa to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit
Gene Name:
fdnH
Locus Tag:
PA4811
Molecular weight:
33.8 kDa
General function:
Involved in respiratory electron transport chain
Specific function:
Formate dehydrogenase allows Pseudomonas aeruginosa to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556(FDN) component of the formate dehydrogenase
Gene Name:
fdnI
Locus Tag:
PA4810
Molecular weight:
23.9 kDa
General function:
Involved in catalytic activity
Specific function:
Specific function unknown
Gene Name:
glcD
Locus Tag:
PA5355
Molecular weight:
53.7 kDa
General function:
Involved in oxidoreductase activity, acting on NADH or NADPH
Specific function:
NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient
Gene Name:
nuoA
Locus Tag:
PA2637
Molecular weight:
15 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient
Gene Name:
nuoB
Locus Tag:
PA2638
Molecular weight:
25.4 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in oxidoreductase activity
Specific function:
NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient
Gene Name:
nuoE
Locus Tag:
PA2640
Molecular weight:
18.1 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in oxidation-reduction process
Specific function:
NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone
Gene Name:
nuoH
Locus Tag:
PA2643
Molecular weight:
36.7 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in electron carrier activity
Specific function:
NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient
Gene Name:
nuoI
Locus Tag:
PA2644
Molecular weight:
20.6 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient
Gene Name:
nuoJ
Locus Tag:
PA2645
Molecular weight:
17.6 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in oxidoreductase activity, acting on NADH or NADPH
Specific function:
There are 2 NADH dehydrogenases in Pseudomonas aeruginosa, however only this complex is able to use dNADH (reduced nicotinamide hypoxanthine dinucleotide, deamino-NADH) and dNADH-DB (dimethoxy- 5-methyl-6-decyl-1,4-benzoquinone) as substrates
Gene Name:
nuoK
Locus Tag:
PA2646
Molecular weight:
11 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient
Gene Name:
nuoM
Locus Tag:
PA2648
Molecular weight:
55.7 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient
Gene Name:
nuoN
Locus Tag:
PA2649
Molecular weight:
51.7 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in electron carrier activity
Specific function:
Catalyzes the oxidation of L-aspartate to iminoaspartate
Gene Name:
nadB
Locus Tag:
PA0761
Molecular weight:
60 kDa
Reactions
L-aspartate + O(2) = iminosuccinate + H(2)O(2).
General function:
Involved in iron-sulfur cluster binding
Specific function:
The nitrate reductase enzyme complex allows Pseudomonas aeruginosa to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit
Gene Name:
narH
Locus Tag:
PA3874
Molecular weight:
58.1 kDa
Reactions
Nitrite + acceptor = nitrate + reduced acceptor.
General function:
Involved in nitrate reductase activity
Specific function:
The nitrate reductase enzyme complex allows Pseudomonas aeruginosa to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit
Gene Name:
narI
Locus Tag:
PA3872
Molecular weight:
25 kDa
Reactions
Nitrite + acceptor = nitrate + reduced acceptor.
General function:
Involved in formate dehydrogenase (NAD+) activity
Specific function:
Formate dehydrogenase allows Pseudomonas aeruginosa to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The alpha subunit forms the active site
Gene Name:
fdnG
Locus Tag:
PA4812
Molecular weight:
104.7 kDa
Reactions
Formate + NAD(+) = CO(2) + NADH.
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient
Gene Name:
nuoF
Locus Tag:
PA2641
Molecular weight:
48.7 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in catalytic activity
Specific function:
(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H(+)
Gene Name:
lldD
Locus Tag:
PA4771
Molecular weight:
41.1 kDa
Reactions
(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H(+).
General function:
Involved in oxidoreductase activity, acting on NADH or NADPH
Specific function:
NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient
Gene Name:
nuoC
Locus Tag:
PA2639
Molecular weight:
68.3 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in electron carrier activity
Specific function:
NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient
Gene Name:
nuoG
Locus Tag:
PA2642
Molecular weight:
99 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:
NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient
Gene Name:
nuoL
Locus Tag:
PA2647
Molecular weight:
66.2 kDa
Reactions
NADH + quinone = NAD(+) + quinol.
General function:
Involved in oxidoreductase activity
Specific function:
Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein napC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism
Gene Name:
napA
Locus Tag:
PA1174
Molecular weight:
92.9 kDa
Reactions
Nitrite + acceptor = nitrate + reduced acceptor.
General function:
Involved in malate dehydrogenase (quinone) activity
Specific function:
(S)-malate + a quinone = oxaloacetate + reduced quinone
Gene Name:
mqo
Locus Tag:
PA3452
Molecular weight:
57.2 kDa
Reactions
(S)-malate + a quinone = oxaloacetate + reduced quinone.
General function:
Involved in iron-sulfur cluster binding
Specific function:
Specific function unknown
Gene Name:
glcF
Locus Tag:
PA5353
Molecular weight:
44.7 kDa
General function:
Involved in coenzyme binding
Specific function:
Specific function unknown
Gene Name:
mdaB
Locus Tag:
PA2580
Molecular weight:
22 kDa
General function:
Involved in catalytic activity
Specific function:
Specific function unknown
Gene Name:
glcE
Locus Tag:
PA5354
Molecular weight:
38.2 kDa
General function:
Involved in protein disulfide oxidoreductase activity
Specific function:
Required for disulfide bond formation in some periplasmic proteins such as phoA or ompA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by dsbB. It is required for pilus biogenesis
Gene Name:
dsbA
Locus Tag:
PA5489
Molecular weight:
23.4 kDa
General function:
Involved in methyltransferase activity
Specific function:
Methyltransferase required for the conversion of dimethylmenaquinone (DMKH2) to menaquinone (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2)
Gene Name:
ubiE
Locus Tag:
PA5063
Molecular weight:
28.3 kDa
Reactions
A demethylmenaquinone + S-adenosyl-L-methionine = a menaquinol + S-adenosyl-L-homocysteine.
S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol = S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol.
General function:
Energy production and conversion
Specific function:
Small subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme napC protein, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism
Gene Name:
napB
Locus Tag:
PA1173
Molecular weight:
17.9 kDa
General function:
Involved in protein disulfide oxidoreductase activity
Specific function:
Required for disulfide bond formation in some periplasmic proteins such as phoA or ompA. Acts by oxidizing the dsbA protein
Gene Name:
dsbB
Locus Tag:
PA0538
Molecular weight:
18.1 kDa
General function:
Involved in heme binding
Specific function:
Mediates electron flow from quinones to the napAB complex
Gene Name:
napC
Locus Tag:
PA1172
Molecular weight:
22.7 kDa
General function:
Involved in unfolded protein binding
Specific function:
Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with the NarI subunit on the membrane
Gene Name:
narJ
Locus Tag:
PA3873
Molecular weight:
27.3 kDa