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Literature summary for 1.6.2.2 extracted from

  • Samhan-Arias, A.K.; Fortalezas, S.; Cordas, C.M.; Moura, I.; Moura, J.J.G.; Gutierrez-Merino, C.
    Cytochrome b5 reductase is the component from neuronal synaptic plasma membrane vesicles that generates superoxide anion upon stimulation by cytochrome c (2018), Redox Biol., 15, 109-114 .
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00029
-
ferricytochrome c soluble isoform, pH 7, 37°C Homo sapiens
0.00042
-
ferricytochrome c membrane-bound isoform, pH 7, 37°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
vesicle neuronal synaptic plasma membrane vesicles Rattus norvegicus 31982
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Rattus norvegicus
-
neuron neuronal synaptic plasma membrane vesicles Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome c + NADH + H+
-
Homo sapiens 2 ferrocytochrome c + NAD+
-
?
2 ferricytochrome c + NADH + H+
-
Rattus norvegicus 2 ferrocytochrome c + NAD+
-
?
NADH + H+ + 2 O2
-
Homo sapiens ?
-
?
NADH + H+ + 2 O2
-
Rattus norvegicus ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.17
-
O2 membrane-bound isoform, pH 7, 37°C Homo sapiens
1.37
-
O2 soluble isoform, pH 7, 37°C Homo sapiens

General Information

General Information Comment Organism
physiological function Cb5R can use O2 as an electron acceptor using NADH as substrate. Cb5R uses one NADH molecule to reduce two O2 molecules, leading to production of superoxide anion radicals Rattus norvegicus
physiological function Cb5R can use O2 as an electron acceptor using NADH as substrate. Cb5R uses one NADH molecule to reduce two O2 molecules, leading to production of superoxide anion radicals. Cytochrome c binds to purified Cb5R isoforms with dissociation constants similar to the Km values for the cytochrome c-stimulated superoxide anion radical production by Cb5R isoforms and close to the Km value obtained for the NADH-dependent production of superoxide anion radicals by synaptic plasma membrane vesicles Homo sapiens