EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.7.2.1 | molecular docking simulations with cytochrome c552 or cytochrome c show that hydrophobic interactions favor the formation of complexes where the heme c domain of the enzyme is the principal docking site. Only for cytochrome c552 the preferential areas of contact and Fe-Fe distances between heme groups of the redox partners allow establishing competent electron transfer pathways. The coupling of the enzyme with chemical redox mediators is not energetically favorable | Marinobacter nauticus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.7.2.1 | nitric oxide + H2O + ferricytochrome c552 | Marinobacter nauticus | - |
nitrite + ferrocytochrome c552 + 2 H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.7.2.1 | Marinobacter nauticus | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.7.2.1 | nitric oxide + H2O + ferricytochrome c | - |
Marinobacter nauticus | nitrite + ferrocytochrome c + 2 H+ | - |
? | |
1.7.2.1 | nitric oxide + H2O + ferricytochrome c552 | - |
Marinobacter nauticus | nitrite + ferrocytochrome c552 + 2 H+ | - |
? | |
1.7.2.1 | nitric oxide + H2O + oxidized phenazine methosulfate | phenazine methosulfate can serve as reducing agents and trigger catalytic activity if the assay is performed in relatively long time windows | Marinobacter nauticus | nitrite + reduced phenazine methosulfate + 2 H+ | - |
? | |
1.7.2.1 | nitric oxide + H2O + oxidized phenosafranin | phenosafranin can serve as reducing agents and trigger catalytic activity if the assay is performed in relatively long time windows | Marinobacter nauticus | nitrite + reduced phenosafranin + 2 H+ | - |
? |