EC Number   |
Cofactor |
Reference |
|---|
   1.9.6.1 | cytochrome c552 |
the enzyme is a complex of a 93000 Da polypeptide and a 16000 Da nitrate-oxidizable cytochrome c552, cytochrome c552 contains two c-type heme moieties |
697696 |
| 1.9.6.1 | heme |
a [4Fe-4S] cluster and two c-type hemes form an intramolecular electron transfer chain that deliver electrons to the active site. Residue lysine 56 connects, through hydrogen-bonds, the [4Fe-4S] center to one of the pyranopterin ligands of the Mo-cofactor |
764214 |
| 1.9.6.1 | heme |
contains 1.3 mol heme per mol of protein (assuminga 110-kDa molecular mass) |
697696 |
| 1.9.6.1 | heme |
subunit NapB is a diheme cytochrome c |
697968 |
| 1.9.6.1 | heme |
the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB) |
674891 |
| 1.9.6.1 | molybdenum cofactor |
- |
699015, 741478, 742319, 742486 |
| 1.9.6.1 | molybdenum cofactor |
a Mo-pyranopterin cofactor |
742648 |
| 1.9.6.1 | molybdenum cofactor |
i.e. MoCo, the EPR signature of the MoCo is heterogeneous. The MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation. The inactive form features an open, oxidized pyranopterin, which is closed upon reduction. Distict from that, a slow, reversible inactivation/reactivation process occurs at high nitrate concentration, overview |
741958 |
| 1.9.6.1 | molybdenum cofactor |
synthesis of the Mo-pyranopterin cofactor, overview |
742319 |
| 1.9.6.1 | molybdopterin |
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor |
712967 |
