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Literature summary for 1.7.2.5 extracted from

  • ter Beek, J.; Krause, N.; Reimann, J.; Lachmann, P.; Aedelroth, P.
    The nitric-oxide reductase from Paracoccus denitrificans uses a single specific proton pathway (2013), J. Biol. Chem., 288, 30626-30635 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.7.2.5

Cloned(Commentary)

Cloned (Comment) Organism
gene norB and norC, recombinant expression in Escherichia coli strain JM109 Paracoccus denitrificans

Protein Variants

Protein Variants Comment Organism
D185A site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type Paracoccus denitrificans
D185E site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type Paracoccus denitrificans
D185N site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type Paracoccus denitrificans
E58Q site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type Paracoccus denitrificans
E78F site-directed mutagenesis, the mutant does not express Paracoccus denitrificans
K54A site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type Paracoccus denitrificans
N47F site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type Paracoccus denitrificans
N47L site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type Paracoccus denitrificans
Q394M site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type Paracoccus denitrificans
Q398L site-directed mutagenesis, mutation of a conserved residue involved in the proton transfer, kinetics compared to the wild-type Paracoccus denitrificans

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane an integral membrane protein Paracoccus denitrificans 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Paracoccus denitrificans
Fe2+ heme and non-heme iron Paracoccus denitrificans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 nitric oxide + 2 ferrocytochrome c + 2 H+ Paracoccus denitrificans
-
 nitrous oxide + 2 ferricytochrome c + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Paracoccus denitrificans Q51662 small subunit encoded by gene norC
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli by solubilization with 1% w/v n-dodecyl-beta-D-maltoside, ultracentrifugation, and anion exchange chromatography Paracoccus denitrificans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 nitric oxide + 2 ferrocytochrome c + 2 H+
-
 Paracoccus denitrificans nitrous oxide + 2 ferricytochrome c + H2O
-
 ?
additional information NO reduction takes place in the NorB subunit that contains three redox centers: two b-type hemes (hemes b and b3) and a non-heme iron (FeB). Heme b3 and the non-heme iron form the binuclear center, where nitric oxide is bound and reduced. Determination of reduction rates of the cNOR variants with O2 and NO Paracoccus denitrificans ?
-
 ?

Subunits

Subunits Comment Organism
heterodimer the enzyme forms a complex of two subunits, NorB and NorC. Subunit NorC is a membrane-anchored cytochrome c with one c-type heme, which presumably forms the site of electron entry. Subunit NorB subunit contains three redox centers: two b-type hemes (hemes b and b3) and a non-heme iron (FeB). Heme b3 and the non-heme iron form the binuclear center, where nitric oxide is bound and reduced, NorB homology structure modelling Paracoccus denitrificans

Synonyms

Synonyms Comment Organism
cNOR
-
 Paracoccus denitrificans
cytochrome c-dependent NO reductase
-
 Paracoccus denitrificans
NO reductase
-
 Paracoccus denitrificans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Paracoccus denitrificans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 7.6 assay at Paracoccus denitrificans

Cofactor

Cofactor Comment Organism Structure
cytochrome heme containing Paracoccus denitrificans
heme NO reduction takes place in the NorB subunit that contains three redox centers: two b-type hemes (hemes b and b3) and a non-heme iron (FeB). Heme b3 and the non-heme iron form the binuclear center, where nitric oxide is bound and reduced Paracoccus denitrificans

General Information

General Information Comment Organism
evolution NORs are members of the heme-copper oxidase (HCuO) superfamily Paracoccus denitrificans
additional information roles of conserved residues in the proton transfer, overview Paracoccus denitrificans