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Literature summary for 1.7.5.1 extracted from

  • Giordani, R.; Buc, J.
    Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli (2004), Eur. J. Biochem., 271, 2400-2407.
    View publication on PubMed
Search for more literature for 1.7.5.1

Protein Variants

Protein Variants Comment Organism
additional information mutant enzyme lacking the highest-potential [4Fe-4S] cluster is devoid of menadione activity, but still retains duroquinone activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrate + 2-methyl-1,4-naphthoquinol 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 Escherichia coli nitrite + 2-methyl-1,4-naphthoquinone + H2O
-
 ?
nitrate + tetramethyl-p-benzoquinol 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 Escherichia coli nitrite + tetramethyl-p-benzoquinone + H2O
-
 ?

Synonyms

Synonyms Comment Organism
nitrate reductase A
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
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 Escherichia coli
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 Escherichia coli