EC Number   |
Metals/Ions |
Reference |
|---|
   7.2.1.1 | Fe |
defined by dipole-dipole magnetic interaction measurements, the interspin distance between the [2Fe-2S]+ cluster and the NqrB subunit-bound FMN anion radical is found to be 22.5 A, which means that for the functional electron transfer between these two centers another cofactor, most likely FMN bound to the NqrC subunit, should be located |
696344 |
| 7.2.1.1 | Fe |
enzyme contains a 2Fe-2S center. 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 | Fe |
the enzyme contains 650-780 ng Fe per mg protein, which corresponds to 2.5-3.0 atoms of Fe per enzyme complex. The enzyme bears only the 2Fe-2S cluster as the sole metal-containing prosthetic group |
696157 |
| 7.2.1.1 | Fe |
the enzyme contains one 2Fe-2S center, 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 | Fe |
the enzyme contains one [2Fe-2S] cluster |
696345 |
| 7.2.1.1 | Fe |
the NqrF subunit contains one FAD and a [2Fe2S] cluster and catalyzes the initial oxidation of NADH. The Na+-NQR is proposed to increase the stability of NqrF' by stimulating the maturation of FeS centers |
699385 |
| 7.2.1.1 | Fe-S |
- |
671141 |
| 7.2.1.1 | Fe2+ |
2 [2Fe-2S] clusters iin the NqrF subunit |
725538 |
| 7.2.1.1 | Fe2+ |
2 [2Fe-2S] clusters in the NqrF subunit |
725539 |
| 7.2.1.1 | Fe2+ |
the enzyme contains one FeS cluster |
725448 |
