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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.

Wordmap for 1.7.5.1

Word Map on EC 1.7.5.1 Wordmap for 1.7.5.1

Reaction

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nitrate
+
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a quinol
=
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nitrite
+
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a quinone
+
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H2O

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 Oxidoreductases
         1.7 Acting on other nitrogenous compounds as donors
             1.7.5 With a quinone or similar compound as acceptor
                EC 1.7.5.11.7.5.1 nitrate reductase (quinone)

Cofactor

Cofactor on EC 1.7.5.1 - nitrate reductase (quinone)

for references in articles please use BRENDA:EC1.7.5.1

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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-Naphthoquinone
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2-methylnaphthalene-1,4-dione
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4Fe-4S-center
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bis(molybdopterin guanine dinucleotide)molybdenum cofactor
cytochrome
-
cytochrome b
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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
-
cytochrome c
demethylmenaquinone
DMKH2, endogeneous demethylmenasemiquinone (DMSK) intermediates are stabilized in the enzyme
flavin
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)
menaquinone
-
there are more than one menaquinol binding sites in NarGHI
molybdenum bis-molybdopterin guanine dinucleotide
molybdo-bis(pyranopterin guanine dinucleotide)
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
ubiquinone
[4Fe-4S] cluster
[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)
additional information
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