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Literature summary for 1.7.5.2 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
Search for more literature for 1.7.5.2

Activating Compound

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ copper A containing enzyme with two copper atoms per enzyme complex, the copper content is 26.7 nmol/mg of protein Schinkia azotoformans
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]

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

Organism

Organism UniProt Comment Textmining
Schinkia azotoformans
-
-
-
Schinkia azotoformans NCCB 100003
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no activity with horse heart ferrocytochrome c Schinkia azotoformans ?
-
 ?
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 ?
-
 ?
additional information no activity with horse heart ferrocytochrome c Schinkia azotoformans NCCB 100003 ?
-
 ?
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 ?
-
 ?
nitric oxide + ascorbic acid
-
 Schinkia azotoformans ?
-
 ?
nitric oxide + ascorbic acid
-
 Schinkia azotoformans NCCB 100003 ?
-
 ?
nitric oxide + menaquinol highest activity with menaquinol Schinkia azotoformans nitrous oxide + menaquinone + H2O
-
 ?
nitric oxide + menaquinol highest activity with menaquinol Schinkia azotoformans NCCB 100003 nitrous oxide + menaquinone + H2O
-
 ?

Subunits

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

Synonyms

Synonyms Comment Organism
menaquinol NO reductase
-
 Schinkia azotoformans
menaquinol:NO oxidoreductase
-
 Schinkia azotoformans

Cofactor

Cofactor Comment Organism Structure
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