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Literature summary for 1.7.2.6 extracted from
- Kinetics of reduction by substrate or dithionite and heme-heme electron transfer in the multiheme hydroxylamine oxidoreductase (1984), Eur. J. Biochem., 141, 565-571.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| CO | - |
Nitrosomonas europaea |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Nitrosomonas europaea | - |
- |
- |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | overview: effect of pH on rate of reduction of heme c553 of the enzyme by NH2OH, rate constant for reduction of hemes of the enzyme by dithionite at 2°C and 19°C and by NH2OH or NH2NH2 at 2°C | Nitrosomonas europaea |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 10.5 | - |
rate of reduction of hemes c 553 of the enzyme increases with pH | Nitrosomonas europaea |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 10.5 | - |
enzyme is permanently inactivated above pH 10.5 | Nitrosomonas europaea |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | contains hemes c-553, c-559 and P-460 in the ratio 5:2:1, P-460 is the site of electron entry | Nitrosomonas europaea | |
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