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Literature summary for 1.7.5.1 extracted from

  • Guigliarelli, B.; Magalon, A.; Asso, M.; Bertrand, P.; Frixon, C.; Giordano, G.; Blasco, F.
    Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters (1996), Biochemistry, 35, 4828-4836.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C196A mutation results in the full loss of the four Fe-S clusters and of the Mo-cofactor, leading to inactive enzyme Escherichia coli
C227A mutation results in the full loss of the four Fe-S clusters and of the Mo-cofactor, leading to inactive enzyme Escherichia coli
C263A mutant retains significant nitrate reductase activity. EPR analysis shows that the highest redox potential [4Fe-4S] cluster (center 1) is selectively removed by the C263A mutation Escherichia coli
C26A mutant retains significant nitrate reductase activity. Mutation likely eliminates the lowest potential [4Fe-4S] cluster (center 4) Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe complete coordination of the four Fe-S centers of the beta-subunit from Escherichia coli nitrate reductase Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P11349 and P09152 and P11350 narH: P11349, narG: P09152, narI: P11350
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrate + reduced benzyl viologen
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Escherichia coli nitrite + oxidized benzyl viologen + H2O
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nitrate + tetramethyl-p-benzoquinol i.e. duroquinol Escherichia coli nitrite + tetramethyl-p-benzoquinone + H2O
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