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Information on EC 1.7.5.1 - nitrate reductase (quinone) and Organism(s) Escherichia coli and UniProt Accession P09152
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1.7.5.1 nitrate reductase (quinone)IUBMB Comments
A membrane-bound enzyme which supports anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate. Contains the bicyclic form of the molybdo-bis(molybdopterin guanine dinucleotide) cofactor, iron-sulfur clusters and heme b. Escherichia coli expresses two forms NarA and NarZ, both being comprised of three subunits.
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Word Map
- 1.7.5.1
-
denitrification
-
denitrify
- quinols
-
dissimilatory
- chlorate
- narj
-
narghji
-
molybdoenzyme
-
nitrate-reducing
- menaquinol
-
nitrate-dependent
-
q-site
- stigmatellin
-
menasemiquinone
-
hyscore
- menadiol
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
membrane-bound nitrate reductase, narghi, nitrate reductase a, nitrate reductase z, quinol-nitrate oxidoreductase, quinol:nitrate oxidoreductase, quinol/nitrate oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NarG
NarGHI
nitrate reductase A
quinol:nitrate oxidoreductase
NarGHI
-
-
nitrate reductase A
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nitrate + a quinol = nitrite + a quinone + H2O
electrons flow in the overall thermodynamically downhill direction from menaquinol (MQ) or ubiquinol (UQ) through the two hemes of NarI, the four [Fe-S] clusters of NarH, and then through the single [4Fe-4S] cluster of NarG to the Mo-bisPGD cofactor, where nitrate is reduced to nitrite
nitrate + a quinol = nitrite + a quinone + H2O
electrons flow in the overall thermodynamically downhill direction from menaquinol (MQ) or ubiquinol (UQ) through the two hemes of NarI, the four [Fe-S] clusters of NarH, and then through the single [4Fe-4S] cluster of NarG to the Mo-bisPGD cofactor, where nitrate is reduced to nitrite
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
nitrite:quinone oxidoreductase
A membrane-bound enzyme which supports anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate. Contains the bicyclic form of the molybdo-bis(molybdopterin guanine dinucleotide) cofactor, iron-sulfur clusters and heme b. Escherichia coli expresses two forms NarA and NarZ, both being comprised of three subunits.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nitrate + 2-hydroxy-3-(3-methyl-2-butenyl)-1,4-naphthoquinol
nitrite + 2-hydroxy-3-(3-methyl-2-butenyl)-1,4-naphthoquinone + H2O
-
-
-
?
nitrite + menaquinone + H2O
nitrate + menaquinol
-
-
-
?
nitrite + naphthoquinone + H2O
nitrate + naphthoquinol
-
-
-
?
nitrate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
nitrite + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone + H2O
-
i.e. decylubiquinol
-
-
?
nitrate + 2-hydroxy-3-(3-methyl-2-butenyl)-1,4-naphthoquinol
nitrite + 2-hydroxy-3-(3-methyl-2-butenyl)-1,4-naphthoquinone + H2O
-
-
-
-
?
nitrate + 5-hydroxy-2-methyl-1,4-naphthoquinol
nitrite + 5-hydroxy-2-methyl-1,4-naphthoquinone + H2O
-
-
-
-
?
nitrate + 5-hydroxy-2-methyl-naphthalene-1,4-diol
nitrite + 5-hydroxy-2-methyl-naphthalene-1,4-dione + H2O
nitrate + duroquinol
nitrite + duroquinone + H2O
-
if quinols are used as the electron donor the enzyme operates by a two-site, enzyme-substitution mechanism
-
-
?
nitrate + quinol
nitrite + quinone
-
NarGHI strongly stabilizes a semiquinone radical located within the dihemic anchor subunit NarI. The semiquinone is located within the quinol oxidation site QD
-
-
?
nitrite + menaquinone + H2O
nitrate + menaquinol
-
-
-
?
nitrite + naphthoquinone + H2O
nitrate + naphthoquinol
-
-
-
?
nitrite + demethylmenaquinone + H2O
nitrate + demethylmenaquinol
-
-
-
?
nitrite + demethylmenaquinone + H2O
nitrate + demethylmenaquinol
endogeneous demethylmenasemiquinone (DMSK) intermediates are stabilized in the enzyme. DMSK is formed at the NarGHI QD quinol oxidation site
-
-
?
nitrate + 2-methyl-1,4-naphthoquinol
nitrite + 2-methyl-1,4-naphthoquinone + H2O
-
i.e menadiol
-
-
?
nitrate + 2-methyl-1,4-naphthoquinol
nitrite + 2-methyl-1,4-naphthoquinone + H2O
-
i.e. menadiol
-
-
?
nitrate + 2-methyl-1,4-naphthoquinol
nitrite + 2-methyl-1,4-naphthoquinone + H2O
i.e. menadiol
-
-
?
nitrate + 2-methyl-1,4-naphthoquinol
nitrite + 2-methyl-1,4-naphthoquinone + H2O
-
i.e. menadiol. As the reduction of nitrate to nitrite requires two electrons, there must necessarily be two successive bindings of quinone, with transfer of one electron to the hemes, then to the [Fe-S] cluster, to be finally accumulated at the level of the molybdenum cofactor to be able to undertake the catalytic reaction. There are two distinct reactions, depending on whether the hemes were previously reduced by menadiol or by duroquinol. A two-pathway electron transfer model for nitrate reductase A is proposed
-
-
?
nitrate + 2-methyl-1,4-naphthoquinol
nitrite + 2-methyl-1,4-naphthoquinone + H2O
-
i.e. menadiol. Electrons from menadiol oxidation are transferred initially to heme bL
-
-
?
nitrate + 5-hydroxy-1,4-naphthoquinol
nitrite + 5-hydroxy-1,4-naphthoquinone + H2O
-
i.e. juglone
-
-
?
nitrate + 5-hydroxy-1,4-naphthoquinol
nitrite + 5-hydroxy-1,4-naphthoquinone + H2O
-
i.e. reduced form of juglone
-
-
?
nitrate + 5-hydroxy-2-methyl-naphthalene-1,4-diol
nitrite + 5-hydroxy-2-methyl-naphthalene-1,4-dione + H2O
-
i.e plumbagin
-
-
?
nitrate + 5-hydroxy-2-methyl-naphthalene-1,4-diol
nitrite + 5-hydroxy-2-methyl-naphthalene-1,4-dione + H2O
-
i.e. reduced form of plumbagin
-
-
?
nitrate + 5-hydroxy-2-methyl-naphthalene-1,4-diol
nitrite + 5-hydroxy-2-methyl-naphthalene-1,4-dione + H2O
-
i.e. reduced form of plumbagin
i.e. plumbagin
-
?
nitrate + quinol
nitrite + quinone + H2O
-
first enzyme involved in respiratory denitrification in prokaryotes
-
-
?
nitrate + quinol
nitrite + quinone + H2O
-
in order to use nitrate as an electron acceptor, Escherichia coli synthesises three distinct enzymes: a membrane-bound enzyme (nitrate reductase A, NarGHI) encoded by the narGHJI operon and a soluble periplasmic nitrate reductase (NapAB, EC 1.9.6.1) encoded by the napFDAGHBC operon. A second membrane-bound nitrate reductase (nitrate reductase Z, NarZYV) encoded by the NarZYWV operon is biochemically similar to NarGHI. Whereas NarGHI synthesis is induced by nitrate under anaerobic conditions, NarZYV is expressed at a cryptic level and may assist Escherichia coli in transition from aerobic to anaerobic respiration (physiological role of this isoenzyme at the onset of the stationary growth phase in rich media). NapAB is mainly expressed in the presence of low concentrations of nitrate under both aerobic and anaerobic conditions, and its expression is suppressed at high nitrate concentrations. Conversely, NarGHI is maximally expressed when nitrate concentration is elevated, and under these conditions becomes the predominant enzyme in Escherichia coli. Thus, NapAB (Ec 1.9.6.1) and NarGHI seem to function in different ranges of nitrate concentration in a complementary way to support anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate
-
-
?
nitrate + quinol
nitrite + quinone + H2O
model of electron transfer in the nitrate reductase: electrons are provided by quinones to the NarI subunit and subsequently transferred to NarH, which eventually delivers them to the molybdenum cofactor where nitrate reduction takes place
-
-
?
nitrate + quinol
nitrite + quinone + H2O
nitrate reductase A reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force
-
-
?
nitrate + quinol
nitrite + quinone + H2O
under anaerobic conditions in the presence of nitrate, Escherichia coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (nitrate reductase A, NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. The arrangement, coordination scheme and unique environment of the redox-active prosthetic groups is revealed
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
-
when reduced viologen dyes act as the electron donor, the enzyme follows a compulsory-order, Theorell-Chance mechanism, in which it is an enzyme-nitrate complex that is reduced rather than the free enzyme
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
when reduced viologen dyes act as the electron donor, the enzyme follows a compulsory-order, Theorell-Chance mechanism, in which it is an enzyme-nitrate complex that is reduced rather than the free enzyme
-
-
?
nitrate + tetramethyl-p-benzoquinol
nitrite + tetramethyl-p-benzoquinone + H2O
-
i.e. duroquinol
-
-
?
nitrate + tetramethyl-p-benzoquinol
nitrite + tetramethyl-p-benzoquinone + H2O
i.e. duroquinol
-
-
?
nitrate + tetramethyl-p-benzoquinol
nitrite + tetramethyl-p-benzoquinone + H2O
-
i.e. duroquinol. As the reduction of nitrate to nitrite requires two electrons, there must necessarily be two successive bindings of quinone, with transfer of one electron to the hemes, then to the [Fe-S] cluster, to be finally accumulated at the level of the molybdenum cofactor to be able to undertake the catalytic reaction. There are two distinct reactions, depending on whether the hemes were previously reduced by menadiol or by duroquinol. A two-pathway electron transfer model for nitrate reductase A is proposed
-
-
?
nitrate + ubiquinol
nitrite + ubiquinone + H2O
-
-
-
?
nitrate + ubiquinol
nitrite + ubiquinone + H2O
-
if quinols are used as the electron donor the enzyme operates by a two-site, enzyme-substitution mechanism
-
-
?
nitrite + demethylmenaquinone + H2O
nitrate + demethylmenaquinol
-
-
-
?
nitrite + demethylmenaquinone + H2O
nitrate + demethylmenaquinol
endogeneous demethylmenasemiquinone (DMSK) intermediates are stabilized in the enzyme. DMSK is formed at the NarGHI QD quinol oxidation site
-
-
?
additional information
?
-
structure-function relationships of quinone reactivity
-
-
?
additional information
?
-
structure-function relationships of quinone reactivity
-
-
?
additional information
?
-
structure-function relationships of quinone reactivity
-
-
?
additional information
?
-
-
structure-function relationships of quinone reactivity
-
-
?
additional information
?
-
-
Escherichia coli expresses two different membrane-bound respiratory nitrate reductases, nitrate reductase A (NRA) and nitrate reductase Z (NRZ). The two enzymes are encoded by distinct operons located within two different loci on the Escherichia coli chromosome. The narGHJI operon, encoding nitrate reductase A, is located in the chlC locus at 27 min, along with several functionally related genes: narK, encoding a nitrate/nitrite antiporter, and the narXL operon, encoding a nitrate-activated, two component regulatory system. The narZYWV operon, encoding nitrate reductase Z, is located in the chlZ locus located at 32.5 min, a region which includes a narK homologue, narU, but no apparent homologue to the narXL operon. The two membrane-bound enzymes have similar structures and biochemical properties and are capable of reducing nitrate using normal physiological substrates. The homology of the amino acid sequences of the peptides encoded by the two operons is extremely high but the intergenic regions share no related sequences. The expression of both the narGHJI operon and the narK gene are positively regulated by two transacting factors Fnr and NarL-phosphate, activated respectively by anaerobiosis and nitrate, while the narZYWV operon and the narU gene are constitutively expressed. Nitrate reductase A, which accounts for 98% of the nitrate reductase activity when fully induced, is clearly the major respiratory nitrate reductase in Escherichia coli
-
-
?
additional information
?
-
-
nitrate reductase Z expression is regulated in a manner opposite to that of nitrate reductase A. The narGHJZ operon is aerobically repressed, strongly induced by nitrate and positively regulated by the fnr gene product. The expression of narZ is anaerobically repressed, induced weakly, if at all, by nitrate and negatively regulated by the fnr gene product. The opposing regulation of these two enzymes suggests that a function of nitrate reductase Z may be to catalyse the immediate flow of electrons to nitrate during an aerobic/anaerobic transition when the bacterium is grown in the presence of nitrate
-
-
?
additional information
?
-
-
NRZ is expressed at a low level that is not influenced by anaerobiosis or nitrate. The NRZ operon is controlled mainly at the level of transcription and is induced 10fold at the onset of stationary phase in rich media. Expression of NRZ nitrate reductase is highly growth phase dependent and is controlled by the alternative vegetative sigma factor RpoS. RpoS-mediated regulation of NRZ may be an important physiological adaptation that allows the cell to use nitrate under stress-associated conditions
-
-
?
additional information
?
-
-
bromate and chlorate are substrates of the enzyme
-
-
?
additional information
?
-
-
the holoenzyme has two independent and spatially distinct active sites, one for quinol oxidation and the other for nitrate reduction
-
-
?
additional information
?
-
structure-function relationships of quinone reactivity
-
-
?
additional information
?
-
structure-function relationships of quinone reactivity
-
-
?
additional information
?
-
structure-function relationships of quinone reactivity
-
-
?
additional information
?
-
-
structure-function relationships of quinone reactivity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nitrite + demethylmenaquinone + H2O
nitrate + demethylmenaquinol
-
-
-
?
nitrite + demethylmenaquinone + H2O
nitrate + demethylmenaquinol
-
-
-
?
nitrate + quinol
nitrite + quinone + H2O
-
first enzyme involved in respiratory denitrification in prokaryotes
-
-
?
nitrate + quinol
nitrite + quinone + H2O
-
in order to use nitrate as an electron acceptor, Escherichia coli synthesises three distinct enzymes: a membrane-bound enzyme (nitrate reductase A, NarGHI) encoded by the narGHJI operon and a soluble periplasmic nitrate reductase (NapAB, EC 1.9.6.1) encoded by the napFDAGHBC operon. A second membrane-bound nitrate reductase (nitrate reductase Z, NarZYV) encoded by the NarZYWV operon is biochemically similar to NarGHI. Whereas NarGHI synthesis is induced by nitrate under anaerobic conditions, NarZYV is expressed at a cryptic level and may assist Escherichia coli in transition from aerobic to anaerobic respiration (physiological role of this isoenzyme at the onset of the stationary growth phase in rich media). NapAB is mainly expressed in the presence of low concentrations of nitrate under both aerobic and anaerobic conditions, and its expression is suppressed at high nitrate concentrations. Conversely, NarGHI is maximally expressed when nitrate concentration is elevated, and under these conditions becomes the predominant enzyme in Escherichia coli. Thus, NapAB (Ec 1.9.6.1) and NarGHI seem to function in different ranges of nitrate concentration in a complementary way to support anaerobic respiration on nitrate under anaerobic conditions and in the presence of nitrate
-
-
?
nitrate + quinol
nitrite + quinone + H2O
model of electron transfer in the nitrate reductase: electrons are provided by quinones to the NarI subunit and subsequently transferred to NarH, which eventually delivers them to the molybdenum cofactor where nitrate reduction takes place
-
-
?
nitrate + quinol
nitrite + quinone + H2O
nitrate reductase A reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force
-
-
?
nitrate + quinol
nitrite + quinone + H2O
under anaerobic conditions in the presence of nitrate, Escherichia coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (nitrate reductase A, NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. The arrangement, coordination scheme and unique environment of the redox-active prosthetic groups is revealed
-
-
?
additional information
?
-
-
Escherichia coli expresses two different membrane-bound respiratory nitrate reductases, nitrate reductase A (NRA) and nitrate reductase Z (NRZ). The two enzymes are encoded by distinct operons located within two different loci on the Escherichia coli chromosome. The narGHJI operon, encoding nitrate reductase A, is located in the chlC locus at 27 min, along with several functionally related genes: narK, encoding a nitrate/nitrite antiporter, and the narXL operon, encoding a nitrate-activated, two component regulatory system. The narZYWV operon, encoding nitrate reductase Z, is located in the chlZ locus located at 32.5 min, a region which includes a narK homologue, narU, but no apparent homologue to the narXL operon. The two membrane-bound enzymes have similar structures and biochemical properties and are capable of reducing nitrate using normal physiological substrates. The homology of the amino acid sequences of the peptides encoded by the two operons is extremely high but the intergenic regions share no related sequences. The expression of both the narGHJI operon and the narK gene are positively regulated by two transacting factors Fnr and NarL-phosphate, activated respectively by anaerobiosis and nitrate, while the narZYWV operon and the narU gene are constitutively expressed. Nitrate reductase A, which accounts for 98% of the nitrate reductase activity when fully induced, is clearly the major respiratory nitrate reductase in Escherichia coli
-
-
?
additional information
?
-
-
nitrate reductase Z expression is regulated in a manner opposite to that of nitrate reductase A. The narGHJZ operon is aerobically repressed, strongly induced by nitrate and positively regulated by the fnr gene product. The expression of narZ is anaerobically repressed, induced weakly, if at all, by nitrate and negatively regulated by the fnr gene product. The opposing regulation of these two enzymes suggests that a function of nitrate reductase Z may be to catalyse the immediate flow of electrons to nitrate during an aerobic/anaerobic transition when the bacterium is grown in the presence of nitrate
-
-
?
additional information
?
-
-
NRZ is expressed at a low level that is not influenced by anaerobiosis or nitrate. The NRZ operon is controlled mainly at the level of transcription and is induced 10fold at the onset of stationary phase in rich media. Expression of NRZ nitrate reductase is highly growth phase dependent and is controlled by the alternative vegetative sigma factor RpoS. RpoS-mediated regulation of NRZ may be an important physiological adaptation that allows the cell to use nitrate under stress-associated conditions
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
demethylmenaquinone
DMKH2, endogeneous demethylmenasemiquinone (DMSK) intermediates are stabilized in the enzyme
molybdenum bis-molybdopterin guanine dinucleotide
the enzyme binds one molybdenum-bis(molybdopterin guanine dinucleotide), i.e. Mo-bis-MGD, cofactor per subunit
quinone
heme bD is distal to NarGH and constitutes part of the quinone binding and oxidation site (Q-site) through the axially coordinating His66 residue and one of the heme bD propionate groups. Bound quinone participates in hydrogen bonds with both the imidazole of His66 and the heme propionate
[4Fe-4S]-center
a single tetranuclear iron-sulfur [4Fe-4S] cluster, known as FS0, is bound to subunit NarG. NarH contains three [4Fe-4S] clusters (FS1-FS3) and one trinuclear iron-sulfur cluster ([3Fe-4S], FS4)
cytochrome b
-
partial proteolysis of the cytochrome b containing holoenzyme by trypsin results in loss of cytochrome b and in cleavage of one of the subunits of the enzyme. The cytochrome-free derivative exhibits a viologen dye dependent activity that is indistinguishable from that of the holoenzyme, but it is incapable of catalyzing the quinol-dependent reaction
-
cytochrome bD
-
NarI is strongly associated with heme bD, Lys86 is required for its stabilization
-
cytochrome bH
-
both heme bL and heme bH are crucial components in the electron-transfer pathway from the subunit NarI through subunit NarH to the catalytic subunit NarG. Without heme bL electrons cannot be transferred from menaquinol to heme bH. On the other hand, in the absence of heme bH, electrons cannot be transferred from the reduced heme bL to the catalytic dimer NarGH. A complex of menadione radical anion associated with the enzyme, is formed during the process of heme reduction by menadiol
-
cytochrome bL
-
both heme bL and heme bH are crucial components in the electron-transfer pathway from the subunit NarI through subunit NarH to the catalytic subunit NarG. Without heme bL electrons cannot be transferred from menaquinol to heme bH. On the other hand, in the absence of heme bH, electrons cannot be transferred from the reduced heme bL to the catalytic dimer NarGH. A complex of menadione radical anion associated with the enzyme, is formed during the process of heme reduction by menadiol
-
demethylmenaquinone
DMKH2, endogeneous demethylmenasemiquinone (DMSK) intermediates are stabilized in the enzyme
heme b
-
the anchor subunit NarI contains two b-type hemes. Electron transfer out of NarI is mediated by two hemes, one of relatively low midpoint potential Em (heme bL), and one of relatively high Em (heme bH)
molybdo-bis(pyranopterin guanine dinucleotide)
Mo-bisPGD cofactor, bound to subunit NarG. NarI anchors the NarGH subunits to the inside of the cytoplasmic membrane and contains two hemes b that are proximal (bP) and distal (bD) to the NarGH subunits, respectively
quinone
heme bD is distal to NarGH and constitutes part of the quinone binding and oxidation site (Q-site) through the axially coordinating His66 residue and one of the heme bD propionate groups. Bound quinone participates in hydrogen bonds with both the imidazole of His66 and the heme propionate
[4Fe-4S]-center
a single tetranuclear iron-sulfur [4Fe-4S] cluster, known as FS0, is bound to subunit NarG. NarH contains three [4Fe-4S] clusters (FS1-FS3) and one trinuclear iron-sulfur cluster ([3Fe-4S], FS4)
heme
the membrane subunit (NarI) of Escherichia coli nitrate reductase A (NarGHI) contains two b-type hemes, both of which are the highly anisotropic low-spin type. Heme bD is distal to NarGH and constitutes part of the quinone binding and oxidation site (Q-site) through the axially coordinating His66 residue and one of the heme bD propionate groups. Bound quinone participates in hydrogen bonds with both the imidazole of His66 and the heme propionate
molybdo-bis(pyranopterin guanine dinucleotide)
Mo-bisPGD cofactor, bound to subunit NarG. NarI anchors the NarGH subunits to the inside of the cytoplasmic membrane and contains two hemes b that are proximal (bP) and distal (bD) to the NarGH subunits, respectively
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
-
evidence for the presence of interactions between the molybdenum cofactor (Moco) biosynthetic machinery and aponitrate reductase A. The final stages of molybdenum cofactor biosynthesis occurs on a complex made up by MogA, MoeA, MobA, and MobB, which is also in charge with the delivery of the mature cofactor onto the aponitrate reductase A in a NarJ-assisted process
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
structural evidence for the role of an open bicyclic form of the molybdo-bis(molybdopterin guanine dinucleotide) cofactor in the catalytic mechanism
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
the enzyme uses a molybdo-bis(molybdopterin guanine dinucleotide) cofactor for catalytic mechanism
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
-
the molybdo-bis(molybdopterin guanine dinucleotide)-binding subunit NarG is organized in four domains around the molybdo-bis(molybdopterin guanine dinucleotide) cofactor
cytochrome
-
although the spectral studies of nitrate reductase Z reveals the presence of a b-type cytochrome subunit (1.5 mol/molecule of 230000 Da), none can be detected in the SDS-PAGE
-
cytochrome
-
NarI is strongly associated with heme bD, Lys86 is required for its stabilization
-
cytochrome
-
the spectrophotometric studies indicate that reduction of the cytochrome hemes varies according to the analogue of quinone used, and in no cases is it complete
-
heme
-
the reduction of NarGHI hemes by menaquinol, the reduction exhibits four phases, a transient species associated with the enzyme is kinetically correlated to the second reduction of the hemes
heme
-
the spectrophotometric studies indicate that reduction of the cytochrome hemes varies according to the analogue of quinone used, and in no cases is it complete
heme
the transmembrane subunit NarI coordinates two low-spin hemes, heme bP and heme bD, which mediate electron transfer from the Q-site to the [Fe-S] clusters in NarH
heme
the membrane subunit (NarI) of Escherichia coli nitrate reductase A (NarGHI) contains two b-type hemes, both of which are the highly anisotropic low-spin type. Heme bD is distal to NarGH and constitutes part of the quinone binding and oxidation site (Q-site) through the axially coordinating His66 residue and one of the heme bD propionate groups. Bound quinone participates in hydrogen bonds with both the imidazole of His66 and the heme propionate
additional information
-
molecular characterization of a quinol binding and oxidation site (Q-site) in NarGHI
-
additional information
-
the semiquinone is located within the quinol oxidation site QD
-
additional information
-
the transmembrane subunit NarI provides the quinol binding and oxidation site (Q-site)
-
additional information
the transmembrane subunit NarI provides the quinol binding and oxidation site (Q-site)
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Molybdenum
the enzyme contains one molybdenum-bis(molybdopterin guanine dinucleotide) cofactor per subunit
Fe
Mo
Fe
complete coordination of the four Fe-S centers of the beta-subunit from Escherichia coli nitrate reductase
Fe
-
coordination model for the four [Fe-S] centres of the electron-transfer subunit NarH, coordination scheme of the [Fe-S] clusters, functional role of [Fe-S] centres
Fe
cysteine arrangements typical of iron-sulfur centers are found in the NarH polypeptide. This suggests that the latter is an electron transfer unit of the nitrate reductase complex
Fe
domain I of subunit NarG holds the [4Fe-4S] cluster FS0. The coordination scheme of FS0 is: His50, Cys54, Cys58, Cys93. NarH contains three [4Fe-4S] clusters, FS1, FS2, FS3 and one [3Fe-4S] cluster, FS4
Fe
domain I of the catalytic subunit NadG holds the [4Fe-4S] cluster FS0
Fe
-
the 230000 Da complex contains 13 atoms iron and 12 atoms labile sulfur/molecules
Fe
-
the catalytic subunit of Escherichia coli nitrate reductase A contains a [4Fe-4S] cluster with a high-spin ground state
Fe
-
the four iron-sulfur centers of nitrate reductase A belong to two classes with markedly different redox potentials. The high-potential group comprises a [3Fe-4S] and a [4Fe-4S] cluster whose midpoint potentials are +60 mV and +80 mV, respectively. Although these centers are magnetically isolated, they are coupled by a significant anticooperative redox interaction of about 50 mV. The [4Fe-4S]1+ center occurs in two different conformations as shown by its composite EPR spectrum. The low-potential group contains two [4Fe-4S] clusters with more typical redox potentials (-200 mV and -400 mV). In the fully reduced state, the three [4Fe-4S]1+ centers are magnetically coupled. The iron-sulfur centers nitrate reductase Z and nitrate reductase A, exhibit essentially the same characteristics, except that the midpoint potentials of the high-potential centers of nitrate reductase Z appear negatively shifted by about 100 mV. A correspondence between the high-potential iron-sulfur clusters of the two enzymes can be proposed
Mo
-
the enzyme contains a molybdenum cofactor. The enzyme-specific chaperone NarJ coordinates assembly and molybdenum cofactor acquisition of the heterotrimeric enzyme during the biogenesis process
Mo
the enzyme uses a molybdo-bis(molybdopterin guanine dinucleotide) cofactor for catalytic mechanism
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethyl dicarbonate
-
the quinol-dependent, but not the viologen dye dependent, activity is inhibited irreversibly by exposure to diethyl pyrocarbonate
additional information
-
p-chloromercuribenzoate (0.5 mM) or 2-heptyl-4-hydroxyquinolin N-oxide (1 mM) are almost without effect on the purified enzyme tested with reduced viologen as electron donor
-
2-n-heptyl-4-hydroxyquinoline N-oxide
-
has significant effects on the reduction kinetics of NarGHIH56R and NarGHIH205Y
2-n-heptyl-4-hydroxyquinoline N-oxide
-
quinol-binding-site inhibitor, elicits a much stronger inhibitory effect than stigmatellin on the reoxidation of the hemes
2-n-heptyl-4-hydroxyquinoline N-oxide
-
the quinol-dependent, but not the viologen dye dependent, activity is inhibited reversibly by treatment with 2-n-heptyl-4-hydroxyquinoline N-oxide
Stigmatellin
-
has significant effects on the reduction kinetics of NarGHIH56R and NarGHIH205Y
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00008
2-n-heptyl-4-hydroxyquinoline N-oxide
Escherichia coli
-
pH 7, substrate: 2-hydroxy-3-(3-methyl-2-butenyl)-1,4-naphthoquinol
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
25
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
NarG and NarH are cytoplasmic subunits
the transmembrane subunit NarI anchors narGH to the cytoplasmic side of the membrane
-
the NarI subunit anchors the NarGH subunits to the inside of the cytoplasmic membrane
-
nitrate reductase A (encoded by narGHJI operon) and nitrate reductase Z (encoded by narZYWv operon) are membrane-bound
-
the enzyme-specific chaperone NarJ controls the quality of the enzyme addressed to the membrane via binding to the N-terminal tail of the iron-sulfur containing subunit NarG
the membrane-intrinsic subunit NarI anchors NarGH to the membrane through a predominantly hydrophobic interface with both subunits
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
quinone site variants Lys86 and Gly65, Q-site inhibitor HOQNO, and their effects on heme bD, overview
metabolism
nitrate enters the periplasm through porins where it is reduced to nitrite by the periplasmic nitrate reductase (Nap) or it is further transported into the bacterial cytosol by NarK and serves as an electron acceptor for nitrate reductase A (NarG). Periplasmic nitrite is further converted to NH3 by the periplasmic nitrite reductase (Nrf). Electrons required for these reactions can be transferred to the quinone (Q) pool by NADH:ubiquinone oxidoreductase (Nuo) in a reaction coupled to energy-conserving proton translocation
malfunction
quinone site variants Lys86 and Gly65, Q-site inhibitor HOQNO, and their effects on heme bD, overview
metabolism
-
demethylmenasemiquinone and menasemiquinone bind in a similar and strongly asymmetric manner through a short H-bond, caused by slightly inequivalent contributions from two beta-methylene protons of the isoprenoid side chain. Their large isotropic hyperfine coupling constants are consistent with both a specific highly asymmetric binding mode of (demethyl)menasemiquinone and a near in-plane orientation of its isoprenyl chain at Cbeta relative to the aromatic ring, which differs by about 90° to that predicted for free or NarGHI-bound menaquinol
physiological function
-
mutants deficient in all three nitrate reductases narGHI, narXYZ, napFDAGHCB are capable of sustaining 48% of protoporphyrinogen IX oxidases activity and 65% of wild-type activity, respectively
additional information
additional information
NarGHI comprises a catalytic subunit (NarG, 140 kDa), an electron-transfer subunit (NarH, 58 kDa), and a membrane anchor subunit (NarI, 26 kDa). NarG contains a Mo-bisPGD cofactor that is the site of nitrate reduction as well as a single tetranuclear iron-sulfur ([4Fe-4S]) cluster known as FS0. NarH contains three [4Fe-4S] clusters (FS1-FS3) and one trinuclear iron-sulfur cluster ([3Fe-4S], FS4). NarI anchors the NarGH subunits to the inside of the cytoplasmic membrane and contains two hemes b that are proximal (bP) and distal (bD) to the NarGH subunits, respectively
additional information
NarGHI comprises a catalytic subunit (NarG, 140 kDa), an electron-transfer subunit (NarH, 58 kDa), and a membrane anchor subunit (NarI, 26 kDa). NarG contains a Mo-bisPGD cofactor that is the site of nitrate reduction as well as a single tetranuclear iron-sulfur ([4Fe-4S]) cluster known as FS0. NarH contains three [4Fe-4S] clusters (FS1-FS3) and one trinuclear iron-sulfur cluster ([3Fe-4S], FS4). NarI anchors the NarGH subunits to the inside of the cytoplasmic membrane and contains two hemes b that are proximal (bP) and distal (bD) to the NarGH subunits, respectively
additional information
NarGHI comprises a catalytic subunit (NarG, 140 kDa), an electron-transfer subunit (NarH, 58 kDa), and a membrane anchor subunit (NarI, 26 kDa). NarG contains a Mo-bisPGD cofactor that is the site of nitrate reduction as well as a single tetranuclear iron-sulfur ([4Fe-4S]) cluster known as FS0. NarH contains three [4Fe-4S] clusters (FS1-FS3) and one trinuclear iron-sulfur cluster ([3Fe-4S], FS4). NarI anchors the NarGH subunits to the inside of the cytoplasmic membrane and contains two hemes b that are proximal (bP) and distal (bD) to the NarGH subunits, respectively
additional information
-
NarGHI comprises a catalytic subunit (NarG, 140 kDa), an electron-transfer subunit (NarH, 58 kDa), and a membrane anchor subunit (NarI, 26 kDa). NarG contains a Mo-bisPGD cofactor that is the site of nitrate reduction as well as a single tetranuclear iron-sulfur ([4Fe-4S]) cluster known as FS0. NarH contains three [4Fe-4S] clusters (FS1-FS3) and one trinuclear iron-sulfur cluster ([3Fe-4S], FS4). NarI anchors the NarGH subunits to the inside of the cytoplasmic membrane and contains two hemes b that are proximal (bP) and distal (bD) to the NarGH subunits, respectively
additional information
structure-function relationships of quinone reactivity. The NarGHI catalytic activity measured with the demethylmenaquinol (DMKH2) analogue 1,4-naphthoquinol is comparable to that measured using the corresponding methylated methylmenaquinol (MKH2) analogue menadiol, kinetics, overview
additional information
structure-function relationships of quinone reactivity. The NarGHI catalytic activity measured with the demethylmenaquinol (DMKH2) analogue 1,4-naphthoquinol is comparable to that measured using the corresponding methylated methylmenaquinol (MKH2) analogue menadiol, kinetics, overview
additional information
structure-function relationships of quinone reactivity. The NarGHI catalytic activity measured with the demethylmenaquinol (DMKH2) analogue 1,4-naphthoquinol is comparable to that measured using the corresponding methylated methylmenaquinol (MKH2) analogue menadiol, kinetics, overview
additional information
-
structure-function relationships of quinone reactivity. The NarGHI catalytic activity measured with the demethylmenaquinol (DMKH2) analogue 1,4-naphthoquinol is comparable to that measured using the corresponding methylated methylmenaquinol (MKH2) analogue menadiol, kinetics, overview
additional information
NarGHI comprises a catalytic subunit (NarG, 140 kDa), an electron-transfer subunit (NarH, 58 kDa), and a membrane anchor subunit (NarI, 26 kDa). NarG contains a Mo-bisPGD cofactor that is the site of nitrate reduction as well as a single tetranuclear iron-sulfur ([4Fe-4S]) cluster known as FS0. NarH contains three [4Fe-4S] clusters (FS1-FS3) and one trinuclear iron-sulfur cluster ([3Fe-4S], FS4). NarI anchors the NarGH subunits to the inside of the cytoplasmic membrane and contains two hemes b that are proximal (bP) and distal (bD) to the NarGH subunits, respectively
additional information
NarGHI comprises a catalytic subunit (NarG, 140 kDa), an electron-transfer subunit (NarH, 58 kDa), and a membrane anchor subunit (NarI, 26 kDa). NarG contains a Mo-bisPGD cofactor that is the site of nitrate reduction as well as a single tetranuclear iron-sulfur ([4Fe-4S]) cluster known as FS0. NarH contains three [4Fe-4S] clusters (FS1-FS3) and one trinuclear iron-sulfur cluster ([3Fe-4S], FS4). NarI anchors the NarGH subunits to the inside of the cytoplasmic membrane and contains two hemes b that are proximal (bP) and distal (bD) to the NarGH subunits, respectively
additional information
NarGHI comprises a catalytic subunit (NarG, 140 kDa), an electron-transfer subunit (NarH, 58 kDa), and a membrane anchor subunit (NarI, 26 kDa). NarG contains a Mo-bisPGD cofactor that is the site of nitrate reduction as well as a single tetranuclear iron-sulfur ([4Fe-4S]) cluster known as FS0. NarH contains three [4Fe-4S] clusters (FS1-FS3) and one trinuclear iron-sulfur cluster ([3Fe-4S], FS4). NarI anchors the NarGH subunits to the inside of the cytoplasmic membrane and contains two hemes b that are proximal (bP) and distal (bD) to the NarGH subunits, respectively
additional information
-
NarGHI comprises a catalytic subunit (NarG, 140 kDa), an electron-transfer subunit (NarH, 58 kDa), and a membrane anchor subunit (NarI, 26 kDa). NarG contains a Mo-bisPGD cofactor that is the site of nitrate reduction as well as a single tetranuclear iron-sulfur ([4Fe-4S]) cluster known as FS0. NarH contains three [4Fe-4S] clusters (FS1-FS3) and one trinuclear iron-sulfur cluster ([3Fe-4S], FS4). NarI anchors the NarGH subunits to the inside of the cytoplasmic membrane and contains two hemes b that are proximal (bP) and distal (bD) to the NarGH subunits, respectively
additional information
structure-function relationships of quinone reactivity. The NarGHI catalytic activity measured with the demethylmenaquinol (DMKH2) analogue 1,4-naphthoquinol is comparable to that measured using the corresponding methylated methylmenaquinol (MKH2) analogue menadiol, kinetics, overview
additional information
structure-function relationships of quinone reactivity. The NarGHI catalytic activity measured with the demethylmenaquinol (DMKH2) analogue 1,4-naphthoquinol is comparable to that measured using the corresponding methylated methylmenaquinol (MKH2) analogue menadiol, kinetics, overview
additional information
structure-function relationships of quinone reactivity. The NarGHI catalytic activity measured with the demethylmenaquinol (DMKH2) analogue 1,4-naphthoquinol is comparable to that measured using the corresponding methylated methylmenaquinol (MKH2) analogue menadiol, kinetics, overview
additional information
-
structure-function relationships of quinone reactivity. The NarGHI catalytic activity measured with the demethylmenaquinol (DMKH2) analogue 1,4-naphthoquinol is comparable to that measured using the corresponding methylated methylmenaquinol (MKH2) analogue menadiol, kinetics, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
138700
x * 138700 + x * 57700, x * 26500, x * 25500, the narGHJI operon that encodes the nitrate reductase encodes four polypeptides NarG (138700 Da), NarH (57700 Da), NarJ (26500 Da) and NarI (25500 Da), calculated from sequence
150000
-
1 * 150000 (alphaz) + 1 * 60000 (betaz) + a b-type cytochrome subunit, SDS-PAGE
223900
multiple isomorphous replacement and anaomalous scattering (MIRAS), crystallographic data
25500
x * 138700 + x * 57700, x * 26500, x * 25500, the narGHJI operon that encodes the nitrate reductase encodes four polypeptides NarG (138700 Da), NarH (57700 Da), NarJ (26500 Da) and NarI (25500 Da), calculated from sequence
26500
x * 138700 + x * 57700, x * 26500, x * 25500, the narGHJI operon that encodes the nitrate reductase encodes four polypeptides NarG (138700 Da), NarH (57700 Da), NarJ (26500 Da) and NarI (25500 Da), calculated from sequence
57700
x * 138700 + x * 57700, x * 26500, x * 25500, the narGHJI operon that encodes the nitrate reductase encodes four polypeptides NarG (138700 Da), NarH (57700 Da), NarJ (26500 Da) and NarI (25500 Da), calculated from sequence
60000
-
1 * 150000 (alphaz) + 1 * 60000 (betaz) + a b-type cytochrome subunit, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
electron transfer can occur from the menaquinol binding site in NarI to the molybdo-bis(molybdopterin guanine dinucleotide) active site in NarG, where nitrate is reduced to nitrite
?
-
1 * 150000 (alphaz) + 1 * 60000 (betaz) + a b-type cytochrome subunit, SDS-PAGE
?
x * 138700 + x * 57700, x * 26500, x * 25500, the narGHJI operon that encodes the nitrate reductase encodes four polypeptides NarG (138700 Da), NarH (57700 Da), NarJ (26500 Da) and NarI (25500 Da), calculated from sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of NarGHI at 1.9 A resolution, crystals of native and selenomethionine-substituted NarGHI are obtained by vapor diffusion with sitting drops
sitting-drop vapor diffusion method, crystals of native and selenomethionine-substituted NarGHI, crystal structure at 1.9 A resolution
the crystal structure of Escherichia coli nitrate reductase A in complex with pentachlorophenol is determined to 2.0 A of resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G65A
site-directed mutageness of subunit NarI, mutant G65A is able to support growth and retains significant quinol:nitrate oxidoreductase activity
H49S
the mutant lacks catalytic activity and the FS0 [4Fe-4S] cluster and molybdo-bis(pyranopterin guanine dinucleotide) cofactor but retains the GDP moieties
R94S
the mutant shows a concomitant decrease in enzyme turnover to about 30% of the wild type
C196A
mutation results in the full loss of the four Fe-S clusters and of the Mo-cofactor, leading to inactive enzyme
C227A
mutation results in the full loss of the four Fe-S clusters and of the Mo-cofactor, leading to inactive enzyme
C263A
mutant retains significant nitrate reductase activity. EPR analysis shows that the highest redox potential [4Fe-4S] cluster (center 1) is selectively removed by the C263A mutation
C26A
mutant retains significant nitrate reductase activity. Mutation likely eliminates the lowest potential [4Fe-4S] cluster (center 4)
G65A
site-directed mutageness of subunit NarI, mutant G65A is able to support growth and retains significant quinol:nitrate oxidoreductase activity
H187Y
H205Y
-
mutant without heme bH but with heme bL, a smaller and slower heme reduction compared to that of the wild-type enzyme is observed. A transient species, likely to be associated with a semiquinone radical anion, is generated not only on reduction of the wild-type enzyme but also on reduction of NarGHIH56R and NarGHIH205Y. Compared to the wild type, no significant heme reoxidation is observed for NarGHIH56R and NarGHIH205Y. This result indicates that a single mutation removing heme bH blocks the electron-transfer pathway from the subunit NarI to the catalytic dimer NarGH
H56R
-
mutant without heme bH but with heme bL, a smaller and slower heme reduction compared to that of the wild-type enzyme is observed. A transient species, likely to be associated with a semiquinone radical anion, is generated not only on reduction of the wild-type enzyme but also on reduction of NarGHIH56R and NarGHIH205Y. Compared to the wild type, no significant heme reoxidation is observed for NarGHIH56R and NarGHIH205Y. This result indicates that a single mutation removing heme bH blocks the electron-transfer pathway from the subunit NarI to the catalytic dimer NarGH
H56Y
H66Y
K86A
additional information
-
mutant enzyme lacking the highest-potential [4Fe-4S] cluster is devoid of menadione activity, but still retains duroquinone activity
H187Y
-
mutant lacking heme bL but having heme bH, the heme reduction by menadiol is abolished
H187Y
-
mutant lacking the distal heme bD, no EPR signal of the semiquinone is observed
H187Y
-
mutant lacks the distal heme bD, no EPR signal of the semiquinone is observed
H56Y
-
a semiquinone is detected in the mutant lacking the proximal heme bP. Its thermodynamic properties and spectroscopic characteristics, as revealed by Q-band EPR and ENDOR spectroscopies, are identical to those observed in the native enzyme
H56Y
-
mutant lacks the distal heme bD, a EPR signal of the semiquinone is observed
H66Y
-
mutant lacking heme bL but having heme bH, the heme reduction by menadiol is abolished
H66Y
-
mutant lacking the distal heme bD, no EPR signal of the semiquinone is observed
H66Y
-
mutant lacks the distal heme bD, no EPR signal of the semiquinone is observed
K86A
-
mutant has a lower plumbagin:nitrate oxidoreductase activity than the wild-type enzyme, 10/s compared with 68/s, respectively
K86A
-
mutation dramatically reduces the rate of oxidation of both menaquinol and ubiquinol analogues
K86A
-
the mutation close to heme bD leads to the loss of the EPR signal of the semiquinone, although both hemes are present, the substitution dramatically reduces the rate of oxidation of both mena and ubiquinol analogues
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing in liquid nitrogen may be repeated up to six times, with a reduction of 20% of the activity
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is remarkably resistant to air inactivation since only 2-5% of the activity is lost after a 1 h treatment
-
697691
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, the purified preparation can be stored up to three days without inactivation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cluster NarGHI, overexpression in Escherichia coli strain LCB79
gene cluster NarGHI, overexpression in Escherichia coli strain LCB79
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
nitrate reductase A is synthesized optimally at NO3- concentrations of 10 mM or above
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morpeth, F.F.; Boxer, D.H.
Kinetic analysis of respiratory nitrate reductase from Escherichia coli K12
Biochemistry
24
40-46
1985
Escherichia coli
Rothery, R.A.; Bertero, M.G.; Cammack, R.; Palak, M.; Blasco, F.; Strynadka, N.C.; Weiner, J.H.
The catalytic subunit of Escherichia coli nitrate reductase A contains a novel [4Fe-4S] cluster with a high-spin ground state
Biochemistry
43
5324-5333
2004
Escherichia coli
Bertero, M.G.; Rothery, R.A.; Boroumand, N.; Palak, M.; Blasco, F.; Ginet, N.; Weiner, J.H.; Strynadka, N.C.
Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A
J. Biol. Chem.
280
14836-14843
2005
Escherichia coli
Vergnes, A.; Pommier, J.; Toci, R.; Blasco, F.; Giordano, G.; Magalon, A.
NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly
J. Biol. Chem.
281
2170-2176
2006
Escherichia coli
Bonnefoy, V.; Demoss, J.A.
Nitrate reductases in Escherichia coli
Antonie van Leeuwenhoek
66
47-56
1994
Escherichia coli
Enoch, H.G.; Lester, R.L.
Role of a novel cytochrome b-containing nitrate reductase and quinone in invitro reconstruction of formate-nitrate reductase activity of E. coli
Biochem. Biophys. Res. Commun.
61
1234-1241
1974
Escherichia coli
Rothery, R.A.; Chatterjee, I.; Kiema, G.; McDermott, M.T.; Weiner, J.H.
Hydroxylated naphthoquinones as substrates for Escherichia coli anaerobic reductases
Biochem. J.
332
35-41
1998
Escherichia coli
Guigliarelli, B.; Magalon, A.; Asso, M.; Bertrand, P.; Frixon, C.; Giordano, G.; Blasco, F.
Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters
Biochemistry
35
4828-4836
1996
Escherichia coli (P11349 and P09152 and P11350), Escherichia coli
Zhao, Z.; Rothery, R.A.; Weiner, J.H.
Effects of site-directed mutations on heme reduction in Escherichia coli nitrate reductase A by menaquinol: a stopped-flow study
Biochemistry
42
14225-14233
2003
Escherichia coli
Zhao, Z.; Rothery, R.A.; Weiner, J.H.
Transient kinetic studies of heme reduction in Escherichia coli nitrate reductase A (NarGHI) by menaquinol
Biochemistry
42
5403-5413
2003
Escherichia coli
Lanciano, P.; Magalon, A.; Bertrand, P.; Guigliarelli, B.; Grimaldi, S.
High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme bD
Biochemistry
46
5323-5329
2007
Escherichia coli
Berks, B.C.; Ferguson, S.J.; Moir, J.W.; Richardson, D.J.
Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions.
Biochim. Biophys. Acta
1232
97-173
1995
Escherichia coli
Vergnes, A.; Gouffi-Belhabich, K.; Blasco, F.; Giordano, G.; Magalon, A.J.
Involvement of the molybdenum cofactor biosynthetic machinery in the maturation of the Escherichia coli nitrate reductase A
Biol. Chem.
279
41398-41403
2004
Escherichia coli
Blasco, F.; Guigliarelli, B.; Magalon, A.; Asso, M.; Giordano, G.; Rothery, RA.
The coordination and function of the redox centres of the membrane-bound nitrate reductases
Cell. Mol. Life Sci.
58
179-193
2001
Escherichia coli
Iobbi-Nivol, C.; Santini, C.L.; Blasco, F.; Giordano, G.
Purification and further characterization of the second nitrate reductase of Escherichia coli K12
Eur. J. Biochem.
188
679-687
1990
Escherichia coli
Guigliarelli, B.; Asso, M.; More, C.; Augier, V.; Blasco, F.; Pommier, J.; Giordano, G.; Bertrand, P.
EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism
Eur. J. Biochem.
207
61-68
1992
Escherichia coli
Giordani, R.; Buc, J.
Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli
Eur. J. Biochem.
271
2400-2407
2004
Escherichia coli
Blasco, F.; Iobbi, C.; Giordano, G.; Chippaux, M.; Bonnefoy, V.
Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer
Mol. Gen. Genet.
218
249-256
1989
Escherichia coli (P09152 and P11349 and P0AF26)
Chang, L.; Wie, L.I.; Audia, J.P.; Morton, R.A.; Schellhorn, H.E.
Expression of the Escherichia coli NRZ nitrate reductase is highly growth phase dependent and is controlled by RpoS, the alternative vegetative sigma factor
Mol. Microbiol.
34
756-766
1999
Escherichia coli
Bertero, M.G.; Rothery, R.A.; Palak, M.; Hou, C.; Lim, D.; Blasco, F.; Weiner, J.H.; Strynadka, N.C.
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A
Nat. Struct. Biol.
10
681-687
2003
Escherichia coli, Escherichia coli (P11349 and P09152 and P11350)
Rothery, R.A.; Bertero, M.G.; Spreter, T.; Bouromand, N.; Strynadka, N.C.; Weiner, J.H.
Protein crystallography reveals a role for the FS0 cluster of Escherichia coli nitrate reductase A (NarGHI) in enzyme maturation
J. Biol. Chem.
285
8801-8807
2010
Escherichia coli (P09152), Escherichia coli, Escherichia coli LCB79 (P09152)
Moebius, K.; Arias-Cartin, R.; Breckau, D.; Haennig, A.L.; Riedmann, K.; Biedendieck, R.; Schroeder, S.; Becher, D.; Magalon, A.; Moser, J.; Jahn, M.; Jahn, D.
Heme biosynthesis is coupled to electron transport chains for energy generation
Proc. Natl. Acad. Sci. USA
107
10436-10441
2010
Escherichia coli
Fedor, J.; Rothery, R.; Weiner, J.
A new paradigm for electron transfer through Escherichia coli nitrate reductase A
Biochemistry
53
4549-4556
2014
Escherichia coli (P09152), Escherichia coli (P11349), Escherichia coli (P11350), Escherichia coli
Rendon, J.; Pilet, E.; Fahs, Z.; Seduk, F.; Sylvi, L.; Hajj Chehade, M.; Pierrel, F.; Guigliarelli, B.; Magalon, A.; Grimaldi, S.
Demethylmenaquinol is a substrate of Escherichia coli nitrate reductase A (NarGHI) and forms a stable semiquinone intermediate at the NarGHI quinol oxidation site
Biochim. Biophys. Acta
1847
739-747
2015
Escherichia coli (P09152), Escherichia coli (P11349), Escherichia coli (P11350), Escherichia coli
Vazquez-Torres, A.; Baeumler, A.J.
Nitrate, nitrite and nitric oxide reductases from the last universal common ancestor to modern bacterial pathogens
Curr. Opin. Microbiol.
29
1-8
2016
Escherichia coli (P09152), Mycobacterium tuberculosis (P9WJQ3), Mycobacterium tuberculosis H37Rv (P9WJQ3), Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZP37)
Seif Eddine, M.; Biaso, F.; Rendon, J.; Pilet, E.; Guigliarelli, B.; Magalon, A.; Grimaldi, S.
1,2H hyperfine spectroscopy and DFT modeling unveil the demethylmenasemiquinone binding mode to E. coli nitrate reductase A (NarGHI)
Biochim. Biophys. Acta Bioenerg.
1861
148203
2020
Escherichia coli
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