Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | the membrane-anchored protein directs electrons from quinol oxidation at the membrane anchor, NarI, to the site of nitrate reduction in the membrane extrinsic [Fe-S] cluster and Mo-bis-MGD containing dimer, NarGH | Paracoccus pantotrophus | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
nitrate + quinol | Paracoccus pantotrophus | the membrane-anchored protein directs electrons from quinol oxidation at the membrane anchor, NarI, to the site of nitrate reduction in the membrane extrinsic [Fe-S] cluster and Mo-bis-MGD containing dimer, NarGH | nitrite + quinone + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paracoccus pantotrophus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
of NarGH | Paracoccus pantotrophus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nitrate + quinol | the membrane-anchored protein directs electrons from quinol oxidation at the membrane anchor, NarI, to the site of nitrate reduction in the membrane extrinsic [Fe-S] cluster and Mo-bis-MGD containing dimer, NarGH | Paracoccus pantotrophus | nitrite + quinone + H2O | - |
? | |
nitrate + reduced methyl viologen | catalysis under substrate-limiting conditions clearly occurs via two pathways with distinct kinetic properties reversibly linked by a redox event. This redox event may be integral to the catalytic cycle of the active site or occur at a center, remote from the description of active-site chemistry, which serves to switch NarGH between two catalytically competent forms | Paracoccus pantotrophus | nitrite + oxidized methyl viologen + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
NarGHI | - |
Paracoccus pantotrophus |
quinol-nitrate oxidoreductase | - |
Paracoccus pantotrophus |