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Literature summary extracted from

  • Suhart, S.; Strampraad, M.; Schröder, I.; De Vries, S.
    A novel copper A containing menaquinol NO reductase from Bacillus azotoformans (2001), Biochemistry, 40, 2632-2639.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.7.5.2 ferricytochrome c NOR activity is stimulated by ferrocytochrome c when phenazine methosulfate and ascorbate are both present Schinkia azotoformans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.7.5.2 cytoplasmic membrane
-
 Schinkia azotoformans
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.5.2 Cu2+ copper A containing enzyme with two copper atoms per enzyme complex, the copper content is 26.7 nmol/mg of protein Schinkia azotoformans
1.7.5.2 Iron the enzyme contains one non-heme iron per enzyme complex. The non-heme iron content is 13.7 nmol/mg Schinkia azotoformans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.5.2 16000
-
 1 * 16000 + 1 * 40000, SDS-PAGE Schinkia azotoformans
1.7.5.2 40000
-
 1 * 16000 + 1 * 40000, SDS-PAGE Schinkia azotoformans
1.7.5.2 112000
-
 gel filtration Schinkia azotoformans

Organism

EC Number Organism UniProt Comment Textmining
1.7.5.2 Schinkia azotoformans
-
-
-
1.7.5.2 Schinkia azotoformans NCCB 100003
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.5.2 Q-Sepharose column chromatography, Sephadex G25 gel filtration, and Bio-Scale Ceramic CHT20-I hydroxyapatite column chromatography Schinkia azotoformans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.7.5.2 0.67
-
 crude membrane extract, pH and temperature not specified in the publication Schinkia azotoformans
1.7.5.2 40.7
-
 after 60.5fold purification, pH and temperature not specified in the publication Schinkia azotoformans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.5.2 additional information no activity with horse heart ferrocytochrome c Schinkia azotoformans ?
-
 ?
1.7.5.2 additional information the activity using sodium borohydride-reduced menaquinone is about 2times higher than obtained in the presence of ascorbic acid, phenazine methosulfate, and horse heart cytochrome c Schinkia azotoformans ?
-
 ?
1.7.5.2 additional information no activity with horse heart ferrocytochrome c Schinkia azotoformans NCCB 100003 ?
-
 ?
1.7.5.2 additional information the activity using sodium borohydride-reduced menaquinone is about 2times higher than obtained in the presence of ascorbic acid, phenazine methosulfate, and horse heart cytochrome c Schinkia azotoformans NCCB 100003 ?
-
 ?
1.7.5.2 nitric oxide + ascorbic acid
-
 Schinkia azotoformans ?
-
 ?
1.7.5.2 nitric oxide + ascorbic acid
-
 Schinkia azotoformans NCCB 100003 ?
-
 ?
1.7.5.2 nitric oxide + menaquinol highest activity with menaquinol Schinkia azotoformans nitrous oxide + menaquinone + H2O
-
 ?
1.7.5.2 nitric oxide + menaquinol highest activity with menaquinol Schinkia azotoformans NCCB 100003 nitrous oxide + menaquinone + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.5.2 heterodimer 1 * 16000 + 1 * 40000, SDS-PAGE Schinkia azotoformans

Synonyms

EC Number Synonyms Comment Organism
1.7.5.2 menaquinol NO reductase
-
 Schinkia azotoformans
1.7.5.2 menaquinol:NO oxidoreductase
-
 Schinkia azotoformans

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.5.2 heme the enzyme contains two b-type hemes per enzyme complex. The heme b content of the purified NO reductase is 25.7 nmol/mg. Heme c is absent Schinkia azotoformans