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Literature summary for 1.7.2.2 extracted from
- Isolation and oligomeric composition of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens (2008), Biochemistry (Moscow), 73, 164-170.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| soluble | - |
Thioalkalivibrio nitratireducens | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | [4Fe-4S]-ferredoxin cofactor | Thioalkalivibrio nitratireducens |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 380000 | 390000 | gel filtration | Thioalkalivibrio nitratireducens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thioalkalivibrio nitratireducens | Q5F2I3 | a haloalkaliphilic bacterium | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme 57.7fold by anion exchange chromatography and gel filtration | Thioalkalivibrio nitratireducens |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 150 | - |
purified native enzyme | Thioalkalivibrio nitratireducens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| nitrite + reduced methyl viologen | - |
Thioalkalivibrio nitratireducens | NH3 + H2O + oxidized methyl viologen | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | determination of the oligomeric composition of NiR by small-angle X-ray scattering, overview | Thioalkalivibrio nitratireducens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cytochrome c nitrite reductase | - |
Thioalkalivibrio nitratireducens |
| NiR | - |
Thioalkalivibrio nitratireducens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Thioalkalivibrio nitratireducens |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 70 | at least 50 h, purified enzyme, stable | Thioalkalivibrio nitratireducens |
| 80 | - |
the half-life is 2.2 h, enzyme inactivation is described by a two-step scheme, about 20% residual activity of after 25 h | Thioalkalivibrio nitratireducens |
| 86 | - |
melting of the TvNiR molecule is an irreversible highly cooperative process with the transition temperature of 86°C and the transition enthalpy of about J/mol of hexamer | Thioalkalivibrio nitratireducens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Thioalkalivibrio nitratireducens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| Ferredoxin | [4Fe-4S]-ferredoxin cofactor | Thioalkalivibrio nitratireducens | |
| methyl viologen | used as the electron donor, reduced with dithionite, artificial cofactor | Thioalkalivibrio nitratireducens | |
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Release 2023.1 (January 2023)
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