Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Chlamydomonas reinhardtii |
Crystallization (Comment) | Organism |
---|---|
modeling of structure based on spinach nitrite reductase. Arginine and lysine residues are involved in electrostatically-stabilized binding to ferredoxin | Chlamydomonas reinhardtii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
63000 | - |
x * 63000, SDS-PAGE | Chlamydomonas reinhardtii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Chlamydomonas reinhardtii | A8J4P1 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
hydroxylamine + reduced ferredoxin | hydroxylamine can serve as an electron-accepting substrate for the enzyme and the product of hydroxylamine reduction is ammonia. Hydroxylamine, bound to the enzyme, can serve as a late intermediate during the reduction of nitrite to ammonia catalyzed by the enzyme | Chlamydomonas reinhardtii | ammonia + H2O + oxidized ferredoxin | - |
? | |
additional information | presence of two separate one-electron redox couples with Em values of -255 mV and -390 mV, respcetively | Chlamydomonas reinhardtii | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 63000, SDS-PAGE | Chlamydomonas reinhardtii |
Synonyms | Comment | Organism |
---|---|---|
Nii1 | - |
Chlamydomonas reinhardtii |