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Literature summary for 1.7.1.1 extracted from

  • Solomonson, L.P.; Barber, M.J.; Robbins, A.P.; Oaks, A.
    Functional domains of assimilatory NADH:nitrate reductase from Chlorella (1986), J. Biol. Chem., 261, 11290-11294.
    View publication on PubMed
Search for more literature for 1.7.1.1

General Stability

General Stability Organism
incubation of the native enzyme with either trypsin, Staphylococcus aureus V8 protease, or a natural inactivator protease from corn results in loss of NADH:nitrate reductase and NADH:cytochrome c reductase activity, but no loss of methyl viologen:nitrate reductase activity Chlorella vulgaris

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum contains 1 molybdenum per subunit Chlorella vulgaris

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
375000
-
-
 Chlorella vulgaris

Organism

Organism UniProt Comment Textmining
Chlorella vulgaris
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricyanide + NADH
-
 Chlorella vulgaris 2 ferrocyanide + NAD+ + H+
-
 ?
2 ferricytochrome c + NADH
-
 Chlorella vulgaris 2 ferrocytochrome c + NAD+ + H+
-
 ?
nitrate + NADH
-
 Chlorella vulgaris nitrite + NAD+ + H2O
-
 ?
reduced methyl viologen + nitrate
-
 Chlorella vulgaris methyl viologen + nitrite
-
 ?

Subunits

Subunits Comment Organism
More FAD/NADH-binding domains exposed on the surface of the molecule, a protease-sensitive hinge region which connects the nitrate-reducing and NADH dehydrogenase moieties, the quarternary structure maintains via association sites on the heme/molybdenum domain Chlorella vulgaris

Cofactor

Cofactor Comment Organism Structure
FAD contains 1 FAD per subunit Chlorella vulgaris
heme contains 1 heme per subunit Chlorella vulgaris
NADH
-
 Chlorella vulgaris