Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state | Paracoccus pantotrophus | |
additional information | cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state | Pseudomonas stutzeri |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paracoccus pantotrophus | P72181 | - |
- |
Pseudomonas stutzeri | P24040 | strain ZoBell ATCC 14405 | - |
Pseudomonas stutzeri ZoBell / ATCC 14405 | P24040 | strain ZoBell ATCC 14405 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state | Paracoccus pantotrophus | ? | - |
? | |
additional information | activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state, reactivity toward nitrite is also observed for oxidized cytochrome cd1 from Pseudomonas stutzeri suggesting a more general involvement of the EPR-silent FeIII heme d1 species in nitrite reduction | Pseudomonas stutzeri | ? | - |
? | |
additional information | activity is associated with histidine/methionine coordination at heme c, and the cytochrome cd1 is activated by exposure to its physiological substrate without the necessity of passing through the reduced state, reactivity toward nitrite is also observed for oxidized cytochrome cd1 from Pseudomonas stutzeri suggesting a more general involvement of the EPR-silent FeIII heme d1 species in nitrite reduction | Pseudomonas stutzeri ZoBell / ATCC 14405 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Paracoccus pantotrophus |
dimer | - |
Pseudomonas stutzeri |
Synonyms | Comment | Organism |
---|---|---|
nitrite reductase | - |
Paracoccus pantotrophus |
nitrite reductase | - |
Pseudomonas stutzeri |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
- |
Pseudomonas stutzeri |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
almost no activity at pH 9.0 | Pseudomonas stutzeri |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome cd1 | cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer. Heme c, which transfers electrons from donor proteins into the active site, has two histidine ligands in the oxidized enzyme from Paracoccus pantotrophus. During reduction of this enzyme, Tyr25 dissociates from the distal side of heme d1, and one heme c ligand is replaced by methionine | Paracoccus pantotrophus | |
cytochrome cd1 | cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer. Heme c, which transfers electrons from donor proteins into the active site, has two histidine ligands in the oxidized enzyme from Paracoccus pantotrophus. During reduction of this enzyme, Tyr25 dissociates from the distal side of heme d1, and one heme c ligand is replaced by methionine. Spectral analysis, overview | Pseudomonas stutzeri | |
heme | cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer | Paracoccus pantotrophus | |
heme | heme c and heme d1, cytochromes cd1 are dimeric bacterial nitrite reductases, which contain two hemes per monomer | Pseudomonas stutzeri |