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Literature summary for 1.7.5.1 extracted from

  • Fedor, J.; Rothery, R.; Weiner, J.
    A new paradigm for electron transfer through Escherichia coli nitrate reductase A (2014), Biochemistry, 53, 4549-4556 .
    View publication on PubMed
Search for more literature for 1.7.5.1

Cloned(Commentary)

Cloned (Comment) Organism
gene cluster NarGHI, overexpression in Escherichia coli strain LCB79 Escherichia coli

Protein Variants

Protein Variants Comment Organism
G65A site-directed mutageness of subunit NarI, mutant G65A is able to support growth and retains significant quinol:nitrate oxidoreductase activity Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the NarI subunit anchors the NarGH subunits to the inside of the cytoplasmic membrane Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nitrite + a quinone + H2O Escherichia coli
-
 nitrate + a quinol
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P09152 NarG
-
Escherichia coli P11349 NarH
-
Escherichia coli P11350 NarI
-

Reaction

Reaction Comment Organism Reaction ID
nitrate + a quinol = nitrite + a quinone + H2O electrons flow in the overall thermodynamically downhill direction from menaquinol (MQ) or ubiquinol (UQ) through the two hemes of NarI, the four [Fe-S] clusters of NarH, and then through the single [4Fe-4S] cluster of NarG to the Mo-bisPGD cofactor, where nitrate is reduced to nitrite Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrite + a quinone + H2O
-
 Escherichia coli nitrate + a quinol
-
 ?

Subunits

Subunits Comment Organism
? x * 140000, NarG subunit, SDS-PAGE Escherichia coli
? x * 26000, NarI subunit, SDS-PAGE Escherichia coli
? x * 58000, NarH subunit, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
gene narH
-
 Escherichia coli
membrane-bound quinol:nitrate oxidoreductase
-
 Escherichia coli
NarG
-
 Escherichia coli
NarGHI
-
 Escherichia coli
NarI
-
 Escherichia coli
nitrate reductase A
-
 Escherichia coli
quinol:nitrate oxidoreductase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme the membrane subunit (NarI) of Escherichia coli nitrate reductase A (NarGHI) contains two b-type hemes, both of which are the highly anisotropic low-spin type. Heme bD is distal to NarGH and constitutes part of the quinone binding and oxidation site (Q-site) through the axially coordinating His66 residue and one of the heme bD propionate groups. Bound quinone participates in hydrogen bonds with both the imidazole of His66 and the heme propionate Escherichia coli
molybdo-bis(pyranopterin guanine dinucleotide) Mo-bisPGD cofactor, bound to subunit NarG. NarI anchors the NarGH subunits to the inside of the cytoplasmic membrane and contains two hemes b that are proximal (bP) and distal (bD) to the NarGH subunits, respectively Escherichia coli
quinone heme bD is distal to NarGH and constitutes part of the quinone binding and oxidation site (Q-site) through the axially coordinating His66 residue and one of the heme bD propionate groups. Bound quinone participates in hydrogen bonds with both the imidazole of His66 and the heme propionate Escherichia coli
[4Fe-4S]-center a single tetranuclear iron-sulfur [4Fe-4S] cluster, known as FS0, is bound to subunit NarG. NarH contains three [4Fe-4S] clusters (FS1-FS3) and one trinuclear iron-sulfur cluster ([3Fe-4S], FS4) Escherichia coli

General Information

General Information Comment Organism
malfunction quinone site variants Lys86 and Gly65, Q-site inhibitor HOQNO, and their effects on heme bD, overview Escherichia coli
additional information NarGHI comprises a catalytic subunit (NarG, 140 kDa), an electron-transfer subunit (NarH, 58 kDa), and a membrane anchor subunit (NarI, 26 kDa). NarG contains a Mo-bisPGD cofactor that is the site of nitrate reduction as well as a single tetranuclear iron-sulfur ([4Fe-4S]) cluster known as FS0. NarH contains three [4Fe-4S] clusters (FS1-FS3) and one trinuclear iron-sulfur cluster ([3Fe-4S], FS4). NarI anchors the NarGH subunits to the inside of the cytoplasmic membrane and contains two hemes b that are proximal (bP) and distal (bD) to the NarGH subunits, respectively Escherichia coli