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Literature summary extracted from

  • Michalski, W.P.; Nicholas, D.J.D.
    Molecular characterization of a copper-containing nitrite reductase from Rhodopseudomonas sphaereoides forma sp. denitrificans (1985), Biochim. Biophys. Acta, 828, 130-137.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.2.1 EDTA 1 mM, complete inhibition after preincubation for 10 min Cereibacter sphaeroides
1.7.2.1 KCN
-
 Cereibacter sphaeroides
1.7.2.1 Urea 4 M, 60% inhibition Cereibacter sphaeroides

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.1 0.0357
-
 nitrite
-
 Cereibacter sphaeroides

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.1 copper one subunit contains a type 1 copper center, the second subunit a type 2 copper center, activity of copper depleted enzyme can be restored Cereibacter sphaeroides

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.2.1 80000
-
 gel filtration, gradient PAGE Cereibacter sphaeroides

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.1 Cereibacter sphaeroides
-
 f. sp. denitrificans
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.2.1 f. sp. denitrificans Cereibacter sphaeroides

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.7.2.1 40
-
 if reduced nitrite is measured Cereibacter sphaeroides
1.7.2.1 80 90 if oxidized benzyl viologen is measured Cereibacter sphaeroides

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.1 N,N-dimethyl-p-phenylenediamine + oxidized benzyl viologen
-
 Cereibacter sphaeroides ?
-
 ?
1.7.2.1 nitrite + ferrocytochrome c artificial electron donor: reduced benzyl viologen Cereibacter sphaeroides nitric oxide + H2O + ferricytochrome c
-
 ?
1.7.2.1 O2-. + H+ purified enzyme shows superoxide dismutase activity, approx. one-third that of pure superoxide dismutase Cereibacter sphaeroides H2O2 + O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.2.1 dimer 2 * 39000-42000, enzyme composed of 2 nonidentical subunits: one contains Cu2+ type 1, the second subunit contains Cu2+ type 2, SDS-PAGE Cereibacter sphaeroides

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.7.2.1 70
-
 activity is not affected after treatment for 10 min, first step in purification Cereibacter sphaeroides