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Literature summary extracted from

  • Gordon, E.H.; Sjogren, T.; Lofqvist, M.; Richter, C.D.; Allen, J.W.; Higham, C.W.; Hajdu, J.; Fulop, V.; Ferguson, S.J.
    Structure and kinetic properties of Paracoccus pantotrophus cytochrome cd1 nitrite reductase with the d1 heme active site ligand tyrosine 25 replaced by serine (2003), J. Biol. Chem., 278, 11773-11781.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.7.2.1 crystals of Y25S mutant protein are grown from a solution containing 10-20 mg/ml protein in the presence of 2.2-2.4 M ammonium sulfate and 50 mM potassium phosphate, pH 7.0, crystals diffract to 1.4 A Paracoccus pantotrophus

Protein Variants

EC Number Protein Variants Comment Organism
1.7.2.1 Y25S unlike the wild-type enzyme, the Y25S mutant is active as a reductase toward nitrite, O2, and hydroxylamine without a reduuctive activation step Paracoccus pantotrophus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.1 0.063
-
 nitrite 25°C, pH 7.0, Y25S mutant enzyme Paracoccus pantotrophus
1.7.2.1 0.071
-
 nitrite 25°C, pH 7.0, activated wild-type enzyme Paracoccus pantotrophus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.1 Iron heme containing enzyme Paracoccus pantotrophus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.2.1 63022
-
 2 * 63022, electrospray mass spectroscopy Paracoccus pantotrophus

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.1 Paracoccus pantotrophus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.2.1 DEAE-Sepharose, Poros HP2, Superdex 200 Paracoccus pantotrophus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.1 hydroxylamine + reduced pseudoazurin
-
 Paracoccus pantotrophus NH3 + H2O + oxidized pseudoazurin
-
 ?
1.7.2.1 nitrite + reduced pseudoazurin
-
 Paracoccus pantotrophus NO + H2O + oxidized pseudoazurin
-
 ?
1.7.2.1 O2 + reduced pseudoazurin
-
 Paracoccus pantotrophus H2O + oxidized pseudoazurin
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.2.1 dimer 2 * 63022, electrospray mass spectroscopy Paracoccus pantotrophus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.7.2.1 2.7
-
 nitrite 25°C, pH 7.0, wild-type, without pre-reduction with dithionite Paracoccus pantotrophus
1.7.2.1 3.2
-
 O2 25°C, pH 7.0, wild-type, pre-reduction with dithionite Paracoccus pantotrophus
1.7.2.1 3.2
-
 hydroxylamine 25°C, pH 7.0, wild-type, pre-reduction with dithionite Paracoccus pantotrophus
1.7.2.1 6.2
-
 O2 25°C, pH 7.0, Y25S mutant enzyme Paracoccus pantotrophus
1.7.2.1 7.7
-
 hydroxylamine 25°C, pH 7.0, Y25S mutant enzyme Paracoccus pantotrophus
1.7.2.1 67
-
 nitrite 25°C, pH 7.0, Y25S mutant enzyme Paracoccus pantotrophus
1.7.2.1 68
-
 nitrite 25°C, pH 7.0, wild-type, pre-reduction with dithionite Paracoccus pantotrophus

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.1 heme c
-
 Paracoccus pantotrophus
1.7.2.1 Heme d1
-
 Paracoccus pantotrophus