Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.5.1.20 extracted from

  • Arnoux, P.; Sabaty, M.; Alric, J.; Frangioni, B.; Guigliarelli, B.; Adriano, J.M.; Pignol, D.
    Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase (2003), Nat. Struct. Biol., 10, 928-934.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure determined at a resolution of 3.2 A Cereibacter sphaeroides

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the diheme electron transfer small subunit NapB binds to the large subunit with heme II in close proximity to the [4Fe-4S] cluster of NapA. The plasticity of the complex contributes to an efficient electron transfer in the complex from the heme I of NapB to the molybdenum catalytic site of NapA Cereibacter sphaeroides
Molybdenum the diheme electron transfer small subunit NapB binds to the large subunit with heme II in close proximity to the [4Fe-4S] cluster of NapA. The plasticity of the complex contributes to an efficient electron transfer in the complex from the heme I of NapB to the molybdenum catalytic site of NapA Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Cereibacter sphaeroides the enzyme is responsible for the first step in the denitrification process ?
-
?

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Cereibacter sphaeroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is responsible for the first step in the denitrification process Cereibacter sphaeroides ?
-
?
nitrate + reduced methyl viologen
-
Cereibacter sphaeroides nitrite + methyl viologen
-
?

Synonyms

Synonyms Comment Organism
NapAB
-
Cereibacter sphaeroides
respiratory nitrate reductase
-
Cereibacter sphaeroides

Cofactor

Cofactor Comment Organism Structure
heme the diheme electron transfer small subunit NapB binds to the large subunit with heme II in close proximity to the [4Fe-4S] cluster of NapA. The plasticity of the complex contributes to an efficient electron transfer in the complex from the heme I of NapB to the molybdenum catalytic site of NapA Cereibacter sphaeroides