EC Number   |
Cofactor |
Reference |
|---|
   7.2.1.1 | FAD |
- |
671141, 671351, 711991, 711994, 711997, 712274, 712407, 741981 |
| 7.2.1.1 | FAD |
complex contains one non-covalently bound FAD, one noncovalently bound riboflavin, ubiquinone-8 and a [2Fe2S] cluster. The phosphate group is attached at the 5'-position of the ribityl as in authentic FMN and the NADH:quinone oxidoreductase contains approximately 1.7 mol covalently bound FMN per mol non-covalently bound FAD |
731327 |
| 7.2.1.1 | FAD |
contains one molecule of covalently bound FAD, believed to be bound to subunit F |
392715 |
| 7.2.1.1 | FAD |
contains one noncovalently bound FAD |
658029, 713414 |
| 7.2.1.1 | FAD |
electrons flow from NADH to quinone through the FAD in subunit F, the 2Fe-2S center, the FMN in subunit C, the FMN in subunit B, and finally riboflavin. The reduction of the FMN(C) to its anionic flavosemiquinone state is the first Na+-dependent process, suggesting that reduction of this site is linked to Na+ uptake. During the reduction reaction, two FMNs are transformed to their anionic flavosemiquinone in a single kinetic step. Subsequently, FMN(C) is converted to the flavohydroquinone, accounting for the single anionic flavosemiquinone radical in the fully reduced enzyme |
698995 |
| 7.2.1.1 | FAD |
enzyme contains FAD |
392695 |
| 7.2.1.1 | FAD |
enzyme contains noncovalently bound FAD |
392713 |
| 7.2.1.1 | FAD |
enzyme contains one molecule of noncovalently bound FAD |
392715 |
| 7.2.1.1 | FAD |
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) contains one noncovalently bound FAD molecule in subunit NqrF. The enzyme shows dependence on covalently bound flavin. ApbE is a modifying enzyme involved in the maturation of flavoproteins, which catalyzes Mg2+-dependent FMN transfer from FAD to Thr residues of flavoproteins in vitro and in vivo, ApbE is the only protein factor required for NqrC flavinylation. Flavinylation o f NqrC is Mg2+-dependent and proceeds with FAD but not FMN |
742842 |
| 7.2.1.1 | FAD |
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) contains one noncovalently bound FAD molecule in subunit NqrF. The enzyme shows dependence on covalently bound flavin. ApbE is a modifying enzyme involved in the maturation of flavoproteins, which catalyzes Mg2+-dependent FMN transfer from FAD to Thr residues of flavoproteins in vitro and in vivo, it catalyzes the flavinylation of truncated Vibrio harveyi NqrCsubunit of enzyme Na+-NQR at Thr229, ApbE is the only protein factor required for NqrC flavinylation. Flavinylation o fNqrC isMg2-dependent and proceeds with FAD but not FMN |
742842 |
