Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe | the enzyme contains one [2Fe-2S] cluster | Vibrio harveyi |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Vibrio harveyi | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
Na+-NQR | - |
Vibrio harveyi |
Na+-translocating NADH:quinone oxidoreductase | - |
Vibrio harveyi |
NADH:quinone oxidoreductase | - |
Vibrio harveyi |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | the enzyme contains four flavin cofactors. The two-electron reduction of the FAD located in the NqrF subunit is coupled with the uptake of only one H+. The one-electron reduction of neutral semiquinone of riboflavin and the formation of anion flavosemiquinone from the oxidized FMN bound to the NqrB subunit are not coupled to any proton uptake. The two sequential one-electron reductions of the FMN residue bound to the NqrC subunit show pH-independent formation of anion radical in the first step and the formation of fully reduced flavin coupled to the uptake of one H+ in the second step. All four flavins stays in the anionic form in the fully reduced enzyme | Vibrio harveyi | |
FMN | the enzyme contains four flavin cofactors. The two-electron reduction of the FAD located in the NqrF subunit is coupled with the uptake of only one H+. The one-electron reduction of neutral semiquinone of riboflavin and the formation of anion flavosemiquinone from the oxidized FMN bound to the NqrB subunit are not coupled to any proton uptake. The two sequential one-electron reductions of the FMN residue bound to the NqrC subunit show pH-independent formation of anion radical in the first step and the formation of fully reduced flavin coupled to the uptake of one H+ in the second step. All four flavins stayed in the anionic form in the fully reduced enzyme | Vibrio harveyi | |
riboflavin | the enzyme contains four flavin cofactors. The two-electron reduction of the FAD located in the NqrF subunit is coupled with the uptake of only one H+. The one-electron reduction of neutral semiquinone of riboflavin and the formation of anion flavosemiquinone from the oxidized FMN bound to the NqrB subunit are not coupled to any proton uptake. The two sequential one-electron reductions of the FMN residue bound to the NqrC subunit show pH-independent formation of anion radical in the first step and the formation of fully reduced flavin coupled to the uptake of one H+ in the second step. All four flavins stays in the anionic form in the fully reduced enzyme | Vibrio harveyi |