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Literature summary for 1.9.6.1 extracted from

  • Jacques, J.G.; Burlat, B.; Arnoux, P.; Sabaty, M.; Guigliarelli, B.; Leger, C.; Pignol, D.; Fourmond, V.
    Kinetics of substrate inhibition of periplasmic nitrate reductase (2014), Biochim. Biophys. Acta, 1837, 1801-1809 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
nitrate at high substrate concentration, substrate inhibition occurs, mechanism of substrate inhibition in Nap, and kinetics, overview Cereibacter sphaeroides

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetics during activation and inactivation of the enzyme, chronoamperometry, overview. The inactive species exists under three redox states, and the active form must exist in different redox states within the catalytic cycle Cereibacter sphaeroides

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Cereibacter sphaeroides
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum within the molybdenum cofactor. The coordination sphere of the Mo ion consists of the four thiolate ligands of two pyranopterins, a sulfur atom from a cysteine that attaches the MoCo to the protein backbone, and a sixth inorganic ligand, proposed to be oxygen or more recently sulfur Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ferrocytochrome + 2 H+ + nitrate Cereibacter sphaeroides
-
2 ferricytochrome + nitrite
-
?
2 ferrocytochrome + 2 H+ + nitrate Cereibacter sphaeroides DSM 158
-
2 ferricytochrome + nitrite
-
?

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides Q53176
-
-
Cereibacter sphaeroides DSM 158 Q53176
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferrocytochrome + 2 H+ + nitrate
-
Cereibacter sphaeroides 2 ferricytochrome + nitrite
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
Cereibacter sphaeroides DSM 158 2 ferricytochrome + nitrite
-
?
additional information the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation Cereibacter sphaeroides ?
-
?
additional information the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation Cereibacter sphaeroides DSM 158 ?
-
?

Subunits

Subunits Comment Organism
heterodimer
-
Cereibacter sphaeroides

Synonyms

Synonyms Comment Organism
NapA
-
Cereibacter sphaeroides
periplasmic nitrate reductase
-
Cereibacter sphaeroides

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Cereibacter sphaeroides

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Cereibacter sphaeroides

Cofactor

Cofactor Comment Organism Structure
cytochrome c two surface-exposed c-type hemes, NapB Cereibacter sphaeroides
molybdenum cofactor i.e. MoCo, the EPR signature of the MoCo is heterogeneous. The MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation. The inactive form features an open, oxidized pyranopterin, which is closed upon reduction. Distict from that, a slow, reversible inactivation/reactivation process occurs at high nitrate concentration, overview Cereibacter sphaeroides
[4Fe-4S] cluster in close proximity to the MoCo Cereibacter sphaeroides

General Information

General Information Comment Organism
evolution the enzyme belongs to the DMSO reductase family Cereibacter sphaeroides