1.7.5.1: nitrate reductase (quinone)
This is an abbreviated version!
For detailed information about nitrate reductase (quinone), go to the full flat file.
Word Map on EC 1.7.5.1
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1.7.5.1
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denitrification
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denitrify
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quinols
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dissimilatory
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chlorate
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narj
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narghji
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molybdoenzyme
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nitrate-reducing
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menaquinol
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nitrate-dependent
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q-site
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stigmatellin
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menasemiquinone
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hyscore
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menadiol
- 1.7.5.1
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denitrification
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denitrify
- quinols
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dissimilatory
- chlorate
- narj
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narghji
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molybdoenzyme
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nitrate-reducing
- menaquinol
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nitrate-dependent
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q-site
- stigmatellin
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menasemiquinone
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hyscore
- menadiol
Reaction
Synonyms
EC 1.7.99.4, gene narH, membrane-bound nitrate reductase, membrane-bound quinol:nitrate oxidoreductase, MSMEG_5140, NaR, NaR1, NarG, NarGHI, narH, NarI, NarZ, nitrate reducatse A, nitrate reductase A, nitrate reductase Z, NRA nitrate reductase A, NRZ, NRZ nitrate reductase, Pden_4236, quinol-nitrate oxidoreductase, quinol/nitrate oxidoreductase, quinol:nitrate oxidoreductase, SCO6532, SCO6533, SCO6534, SCO6535
ECTree
1.7.5.1 nitrate reductase (quinone)Advanced search results
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results (Cofactor
Cofactor on EC 1.7.5.1 - nitrate reductase (quinone)
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
cytochrome bD
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NarI is strongly associated with heme bD, Lys86 is required for its stabilization
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cytochrome bH
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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
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cytochrome bL
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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
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demethylmenaquinone
DMKH2, endogeneous demethylmenasemiquinone (DMSK) intermediates are stabilized in the enzyme
heme b
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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)
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)
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
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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
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the enzyme possesses a molybdopterin guanine dinucleotide active center. Two forms of the molybdenum center, high- and low-pH, are detectable by electron paramagnetic resonance spectroscopy
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
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the molybdo-bis(molybdopterin guanine dinucleotide)-binding subunit NarG is organized in four domains around the molybdo-bis(molybdopterin guanine dinucleotide) cofactor
cytochrome
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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
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cytochrome
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NarI is strongly associated with heme bD, Lys86 is required for its stabilization
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cytochrome
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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
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cytochrome b
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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
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cytochrome b
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the enzyme contains two b-type hemes in the gamma subunit. The two b-type centres are functional parts of the enzyme
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cytochrome c
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NarC contains a periplasmic cytochrome c, which is required for membrane attachment and maturation of the NarG catalytic subunit of the enzyme
cytochrome c
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the isolated preparation contains heme c in a sub-stoichiometric amount with the ability to relay electrons to the molybdenum center, suggesting that this nitrate reductase may contain heme c instead of the heme b usually found in this class of enzymes
heme
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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
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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
molybdenum bis-molybdopterin guanine dinucleotide
the enzyme binds one molybdenum-bis(molybdopterin guanine dinucleotide), i.e. Mo-bis-MGD, cofactor per subunit
molybdenum bis-molybdopterin guanine dinucleotide
the enzyme binds one molybdenum-bis(molybdopterin guanine dinucleotide), i.e. Mo-bis-MGD, cofactor per subunit
molybdenum bis-molybdopterin guanine dinucleotide
the enzyme binds one molybdenum-bis(molybdopterin guanine dinucleotide), i.e. Mo-bis-MGD, cofactor per subunit
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
[4Fe-4S] cluster
the enzyme binds one [4Fe-4S] cluster per subunit
[4Fe-4S] cluster
the enzyme binds one [4Fe-4S] cluster per subunit
additional information
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molecular characterization of a quinol binding and oxidation site (Q-site) in NarGHI
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additional information
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the semiquinone is located within the quinol oxidation site QD
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additional information
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the transmembrane subunit NarI provides the quinol binding and oxidation site (Q-site)
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additional information
the transmembrane subunit NarI provides the quinol binding and oxidation site (Q-site)
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