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Literature summary for 1.7.5.1 extracted from

  • Morpeth, F.F.; Boxer, D.H.
    Kinetic analysis of respiratory nitrate reductase from Escherichia coli K12 (1985), Biochemistry, 24, 40-46.
    View publication on PubMed
Search for more literature for 1.7.5.1

Inhibitors

Inhibitors Comment Organism Structure
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 Escherichia coli
diethyl dicarbonate the quinol-dependent, but not the viologen dye dependent, activity is inhibited irreversibly by exposure to diethyl pyrocarbonate Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Escherichia coli 16020
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the holoenzyme has two independent and spatially distinct active sites, one for quinol oxidation and the other for nitrate reduction Escherichia coli ?
-
 ?
nitrate + duroquinol if quinols are used as the electron donor the enzyme operates by a two-site, enzyme-substitution mechanism Escherichia coli nitrite + duroquinone + H2O
-
 ?
nitrate + reduced benzyl viologen 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 Escherichia coli nitrite + oxidized benzyl viologen + H2O
-
 ?
nitrate + reduced methyl viologen 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 Escherichia coli nitrite + oxidized methyl viologen + H2O
-
 ?
nitrate + ubiquinol if quinols are used as the electron donor the enzyme operates by a two-site, enzyme-substitution mechanism Escherichia coli nitrite + ubiquinone + H2O
-
 ?

Cofactor

Cofactor Comment Organism Structure
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 Escherichia coli