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Literature summary for 1.9.6.1 extracted from

  • Brondijk, T.H.; Fiegen, D.; Richardson, D.J.; Cole, J.A.
    Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation (2002), Mol. Microbiol., 44, 245-255.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
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Escherichia coli K-12
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-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nitrate + ferrocytochrome Escherichia coli K-12 NapG and H, but not NapF, are essential for electron transfer from ubiquinol to NapAB. NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB. It is proposed that NapG and H form an energy conserving quinol dehydrogenase functioning as either components of a proton pump or in a Q cycle, as electrons are transferred from ubiquinol to the membrane-bound cytochrome NapC nitrite + ferricytochrome + H2O
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli K-12
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrate + ferrocytochrome NapG and H, but not NapF, are essential for electron transfer from ubiquinol to NapAB. NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB. It is proposed that NapG and H form an energy conserving quinol dehydrogenase functioning as either components of a proton pump or in a Q cycle, as electrons are transferred from ubiquinol to the membrane-bound cytochrome NapC Escherichia coli K-12 nitrite + ferricytochrome + H2O
-
?
nitrate + ferrocytochrome the membrane-bound cytochrome NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB Escherichia coli K-12 nitrite + ferricytochrome + H2O
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?

Subunits

Subunits Comment Organism
More the nap operon of Escherichia coli K-12, encoding a periplasmic nitrate reductase, encodes seven proteins. The catalytic complex in the periplasm, NapA–NapB receives electrons from the quinol pool via the membrane-bound cytochrome NapC. Like NapA, B and C, NapD, is also essential for Nap activity. None of the remaining three polypeptides, NapF, G and H, which are predicted to encode non-heme, iron-sulfur proteins, are essential for Nap activity Escherichia coli K-12

Synonyms

Synonyms Comment Organism
periplasmic nitrate reductase
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Escherichia coli K-12

Cofactor

Cofactor Comment Organism Structure
cytochrome the membrane-bound cytochrome NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB Escherichia coli K-12